ALGC_PSEAE
ID ALGC_PSEAE Reviewed; 463 AA.
AC P26276;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Phosphomannomutase/phosphoglucomutase;
DE Short=PMM / PGM;
DE EC=5.4.2.2 {ECO:0000269|PubMed:8050998};
DE EC=5.4.2.8 {ECO:0000269|PubMed:8050998};
GN Name=algC; OrderedLocusNames=PA5322;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, FUNCTION AS A
RP PHOSPHOMANNOMUTASE, AND MUTAGENESIS OF ARG-421.
RC STRAIN=8830;
RX PubMed=1903398; DOI=10.1016/s0021-9258(18)92885-1;
RA Zielinski N.A., Chakrabarty A.M., Berry A.;
RT "Characterization and regulation of the Pseudomonas aeruginosa algC gene
RT encoding phosphomannomutase.";
RL J. Biol. Chem. 266:9754-9763(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP FUNCTION AS A PHOSPHOGLUCOMUTASE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1, and PAC1R;
RX PubMed=7515870; DOI=10.1128/jb.176.12.3500-3507.1994;
RA Coyne M.J. Jr., Russell K.S., Coyle C.L., Goldberg J.B.;
RT "The Pseudomonas aeruginosa algC gene encodes phosphoglucomutase, required
RT for the synthesis of a complete lipopolysaccharide core.";
RL J. Bacteriol. 176:3500-3507(1994).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=8830;
RX PubMed=8050998; DOI=10.1128/jb.176.16.4851-4857.1994;
RA Ye R.W., Zielinski N.A., Chakrabarty A.M.;
RT "Purification and characterization of phosphomannomutase/phosphoglucomutase
RT from Pseudomonas aeruginosa involved in biosynthesis of both alginate and
RT lipopolysaccharide.";
RL J. Bacteriol. 176:4851-4857(1994).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10481091; DOI=10.1111/j.1574-6968.1999.tb08712.x;
RA Olvera C., Goldberg J.B., Sanchez R., Soberon-Chavez G.;
RT "The Pseudomonas aeruginosa algC gene product participates in rhamnolipid
RT biosynthesis.";
RL FEMS Microbiol. Lett. 179:85-90(1999).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, POSSIBLE
RP REACTION MECHANISM, MASS SPECTROMETRY, PHOSPHORYLATION, AND MUTAGENESIS OF
RP SER-108.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=11716469; DOI=10.1006/abbi.2001.2618;
RA Naught L.E., Tipton P.A.;
RT "Kinetic mechanism and pH dependence of the kinetic parameters of
RT Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase.";
RL Arch. Biochem. Biophys. 396:111-118(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH METAL OF WILD-TYPE
RP AND ASP-108 MUTANT, DOMAIN, ACTIVE SITE, AND PHOSPHORYLATION AT SER-108.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=11839312; DOI=10.1016/s0969-2126(02)00705-0;
RA Regni C., Tipton P.A., Beamer L.J.;
RT "Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P.
RT aeruginosa virulence factors.";
RL Structure 10:269-279(2002).
RN [8] {ECO:0007744|PDB:1P5D, ECO:0007744|PDB:1P5G, ECO:0007744|PDB:1PCJ, ECO:0007744|PDB:1PCM}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEXES WITH ZINC;
RP ALPHA-D-GLUCOSE-1-PHOSPHATE; ALPHA-D-GLUCOSE-6-PHOSPHATE; ZINC;
RP ALPHA-D-MANNOSE 1-PHOSPHATE AND ALPHA-D-MANNOSE 6-PHOSPHATE, COFACTOR,
RP ACTIVE SITE, PHOSPHORYLATION AT SER-108, AND MUTAGENESIS OF GLU-325.
RX PubMed=14725765; DOI=10.1016/j.str.2003.11.015;
RA Regni C., Naught L., Tipton P.A., Beamer L.J.;
RT "Structural basis of diverse substrate recognition by the enzyme PMM/PGM
RT from P. aeruginosa.";
RL Structure 12:55-63(2004).
RN [9] {ECO:0007744|PDB:2H4L, ECO:0007744|PDB:2H5A}
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEXES WITH ZINC;
RP ALPHA-D-RIBOSE 1-PHOSPHATE AND ALPHA-D-XYLOSE 1-PHOSPHATE, FUNCTION,
RP COFACTOR, ACTIVITY REGULATION, ACTIVE SITE, AND PHOSPHORYLATION AT SER-108.
RX PubMed=16880541; DOI=10.1107/s1744309106025887;
RA Regni C., Shackelford G.S., Beamer L.J.;
RT "Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow
RT substrate and an inhibitor.";
RL Acta Crystallogr. F 62:722-726(2006).
RN [10] {ECO:0007744|PDB:2FKF, ECO:0007744|PDB:2FKM}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-463 IN COMPLEX WITH METAL AND
RP REACTION INTERMEDIATE, FUNCTION, COFACTOR, REACTION MECHANISM,
RP BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION AT SER-108, AND MUTAGENESIS
RP OF ARG-15; ARG-20; ASN-110; ARG-247 AND ARG-421.
RX PubMed=16595672; DOI=10.1074/jbc.m600590200;
RA Regni C., Schramm A.M., Beamer L.J.;
RT "The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural
RT insights into a simple processive enzyme.";
RL J. Biol. Chem. 281:15564-15571(2006).
RN [11] {ECO:0007744|PDB:3BKQ, ECO:0007744|PDB:3C04}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF GLY-368 MUTANT IN COMPLEX WITH
RP METAL OF APOPROTEIN AND IN COMPLEX WITH ALPHA-D-GLUCOSE-1-PHOSPHATE,
RP FUNCTION, COFACTOR, DOMAIN, AND MUTAGENESIS OF ARG-262 AND PRO-368.
RX PubMed=18690721; DOI=10.1021/bi8005219;
RA Schramm A.M., Mehra-Chaudhary R., Furdui C.M., Beamer L.J.;
RT "Backbone flexibility, conformational change, and catalysis in a
RT phosphohexomutase from Pseudomonas aeruginosa.";
RL Biochemistry 47:9154-9162(2008).
RN [12] {ECO:0007744|PDB:3RSM}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF CYS-108 MUTANT IN COMPLEX WITH
RP METAL, FUNCTION, DOMAIN, AND MUTAGENESIS OF SER-108.
RX PubMed=22242625; DOI=10.1021/bi201609n;
RA Sarma A.V., Anbanandam A., Kelm A., Mehra-Chaudhary R., Wei Y., Qin P.,
RA Lee Y., Berjanskii M.V., Mick J.A., Beamer L.J., Van Doren S.R.;
RT "Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility,
RT substates, and phosphoryl transfer defect.";
RL Biochemistry 51:807-819(2012).
RN [13] {ECO:0007744|PDB:4IL8}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF ALA-329 MUTANT IN COMPLEX WITH
RP MAGNESIUM, FUNCTION, COFACTOR, REACTION MECHANISM, ACTIVE SITE, AND
RP MUTAGENESIS OF HIS-329.
RX PubMed=23517223; DOI=10.1111/febs.12249;
RA Lee Y., Mehra-Chaudhary R., Furdui C., Beamer L.J.;
RT "Identification of an essential active-site residue in the alpha-D-
RT phosphohexomutase enzyme superfamily.";
RL FEBS J. 280:2622-2632(2013).
RN [14] {ECO:0007744|PDB:4MRQ}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF DEPHOSPHORYLATED PROTEIN IN
RP COMPLEX WITH METAL, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24403075; DOI=10.1074/jbc.m113.532226;
RA Lee Y., Villar M.T., Artigues A., Beamer L.J.;
RT "Promotion of enzyme flexibility by dephosphorylation and coupling to the
RT catalytic mechanism of a phosphohexomutase.";
RL J. Biol. Chem. 289:4674-4682(2014).
CC -!- FUNCTION: Highly reversible phosphoryltransferase. The
CC phosphomannomutase activity produces a precursor for alginate
CC polymerization, the alginate layer causes a mucoid phenotype and
CC provides a protective barrier against host immune defenses and
CC antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis
CC due to its phosphoglucomutase activity. Essential for rhamnolipid
CC production, an exoproduct correlated with pathogenicity
CC (PubMed:10481091). Required for biofilm production. The reaction
CC proceeds via 2 processive phosphoryl transferase reactions; first from
CC enzyme-phospho-Ser-108 to the substrate (generating a bisphosphorylated
CC substrate intermediate and a dephosphorylated enzyme), a 180 degree
CC rotation of the intermediate (probably aided by movement of domain 4),
CC and subsequent transfer of phosphate back to the enzyme
CC (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625).
CC {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:11716469,
CC ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541,
CC ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:1903398,
CC ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223,
CC ECO:0000269|PubMed:7515870, ECO:0000269|PubMed:8050998}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC EC=5.4.2.8; Evidence={ECO:0000269|PubMed:8050998};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000269|PubMed:8050998};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23517223};
CC Note=Binds 1 Mg(2+) ion per subunit (PubMed:23517223). Zn(2+) can
CC substitute, but yields a catalytically inactive enzyme
CC (PubMed:14725765, PubMed:16880541, PubMed:16595672).
CC {ECO:0000269|PubMed:23517223, ECO:0000305|PubMed:14725765,
CC ECO:0000305|PubMed:16595672, ECO:0000305|PubMed:16880541};
CC -!- ACTIVITY REGULATION: Requires glucose 1,6-bisphosphate (G1,6P) as an
CC activator (PubMed:8050998, PubMed:11716469). Reaction making glucose 6-
CC phosphate is subject to substrate inhibition, reactions making mannose
CC 1-phosphate or glucose 1-phosphate are not. 1-deoxyglucose 6-phosphate
CC competitively inhibits glucose 1-phosphate (PubMed:11716469). Inhibited
CC by xylose 1-phosphate (PubMed:16880541). {ECO:0000269|PubMed:11716469,
CC ECO:0000269|PubMed:8050998, ECO:0000305|PubMed:16880541}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22 uM for glucose 1-phosphate {ECO:0000269|PubMed:8050998};
CC KM=17 uM for mannose 1-phosphate {ECO:0000269|PubMed:8050998};
CC KM=5.4 uM for glucose 1-phosphate {ECO:0000269|PubMed:11716469};
CC KM=0.38 mM for glucose 6-phosphate {ECO:0000269|PubMed:11716469};
CC KM=0.51 mM for mannose 6-phosphate {ECO:0000269|PubMed:11716469};
CC KM=27.3 uM for glucose 6-phosphate {ECO:0000269|PubMed:16595672};
CC Note=kcat is 3000 min(-1) for glucose 1-phosphate and 1350 min(-1)
CC for mannose 1-phosphate. {ECO:0000269|PubMed:8050998};
CC Temperature dependence:
CC TM is 66 degrees Celsius for phosphorylated protein and 62 degrees
CC Celsius for unphosphorylated protein. {ECO:0000269|PubMed:24403075};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 2/2.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8050998}.
CC -!- INDUCTION: By D-mannose 6-phosphate.
CC -!- DOMAIN: Consists of 4 domains; domains 1-3 have a similar toplological
CC core while domain 4 folds over and closes the active site from a hinge
CC region. Mutants in the hinge region (residues 262 and 368-369)
CC generally increase KM for glucose 1-phosphate 2-fold while reducing
CC kcat about 10-fold (PubMed:18690721). {ECO:0000269|PubMed:11839312,
CC ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:22242625}.
CC -!- MASS SPECTROMETRY: Mass=50220; Method=MALDI; Note=May be
CC phosphorylated, protein expressed in E.coli.;
CC Evidence={ECO:0000269|PubMed:11716469};
CC -!- DISRUPTION PHENOTYPE: No longer expresses O-antigen LPS side chain or
CC A-band LPS, sensitive to serum, resistant to virus E79. Has no
CC phosphomannomutase nor phosphoglucomutase activities (PubMed:7515870,
CC PubMed:8050998). Does not make rhamnolipid (PubMed:10481091).
CC {ECO:0000269|PubMed:10481091, ECO:0000269|PubMed:7515870,
CC ECO:0000269|PubMed:8050998}.
CC -!- MISCELLANEOUS: Most crystals have Zn(2+) rather than Mg(2+) and are
CC catalytically inactive. {ECO:0000305|PubMed:14725765,
CC ECO:0000305|PubMed:16595672, ECO:0000305|PubMed:16880541}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; M60873; AAA25701.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08707.1; -; Genomic_DNA.
DR PIR; A40013; A40013.
DR PIR; H82979; H82979.
DR RefSeq; WP_003121305.1; NZ_QZFX01000069.1.
DR PDB; 1K2Y; X-ray; 1.75 A; X=1-463.
DR PDB; 1K35; X-ray; 2.20 A; A=1-463.
DR PDB; 1P5D; X-ray; 1.60 A; X=1-463.
DR PDB; 1P5G; X-ray; 1.61 A; X=1-463.
DR PDB; 1PCJ; X-ray; 2.00 A; X=1-463.
DR PDB; 1PCM; X-ray; 1.90 A; X=1-463.
DR PDB; 2FKF; X-ray; 2.00 A; A=2-463.
DR PDB; 2FKM; X-ray; 1.90 A; X=2-463.
DR PDB; 2H4L; X-ray; 2.40 A; X=1-463.
DR PDB; 2H5A; X-ray; 1.72 A; X=1-463.
DR PDB; 3BKQ; X-ray; 2.05 A; X=1-463.
DR PDB; 3C04; X-ray; 2.20 A; A=1-463.
DR PDB; 3RSM; X-ray; 2.10 A; A=1-463.
DR PDB; 4IL8; X-ray; 1.80 A; A=1-463.
DR PDB; 4MRQ; X-ray; 1.90 A; A=9-463.
DR PDBsum; 1K2Y; -.
DR PDBsum; 1K35; -.
DR PDBsum; 1P5D; -.
DR PDBsum; 1P5G; -.
DR PDBsum; 1PCJ; -.
DR PDBsum; 1PCM; -.
DR PDBsum; 2FKF; -.
DR PDBsum; 2FKM; -.
DR PDBsum; 2H4L; -.
DR PDBsum; 2H5A; -.
DR PDBsum; 3BKQ; -.
DR PDBsum; 3C04; -.
DR PDBsum; 3RSM; -.
DR PDBsum; 4IL8; -.
DR PDBsum; 4MRQ; -.
DR AlphaFoldDB; P26276; -.
DR BMRB; P26276; -.
DR SMR; P26276; -.
DR STRING; 287.DR97_2693; -.
DR DrugBank; DB02007; alpha-D-glucose 6-phosphate.
DR DrugBank; DB02843; alpha-D-glucose-1-phosphate.
DR DrugBank; DB02900; alpha-D-mannose 6-phosphate.
DR DrugBank; DB02867; D-Mannose 1-Phosphate.
DR DrugBank; DB04522; Dexfosfoserine.
DR iPTMnet; P26276; -.
DR PaxDb; P26276; -.
DR PRIDE; P26276; -.
DR EnsemblBacteria; AAG08707; AAG08707; PA5322.
DR PseudoCAP; PA5322; -.
DR HOGENOM; CLU_016950_9_1_6; -.
DR InParanoid; P26276; -.
DR OMA; HSGEINF; -.
DR PhylomeDB; P26276; -.
DR BioCyc; MetaCyc:MON-19202; -.
DR BRENDA; 5.4.2.2; 5087.
DR BRENDA; 5.4.2.8; 5087.
DR SABIO-RK; P26276; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00126; UER00424.
DR EvolutionaryTrace; P26276; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004614; F:phosphoglucomutase activity; IDA:UniProtKB.
DR GO; GO:0004615; F:phosphomannomutase activity; IDA:UniProtKB.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0009243; P:O antigen biosynthetic process; IMP:PseudoCAP.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alginate biosynthesis; Direct protein sequencing; Isomerase;
KW Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW Multifunctional enzyme; Phosphoprotein; Reference proteome; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1903398"
FT CHAIN 2..463
FT /note="Phosphomannomutase/phosphoglucomutase"
FT /id="PRO_0000147814"
FT REGION 13..142
FT /note="Topological domain 1"
FT /evidence="ECO:0000305|PubMed:11839312"
FT REGION 159..255
FT /note="Topological domain 2"
FT /evidence="ECO:0000305|PubMed:11839312"
FT REGION 260..364
FT /note="Topological domain 3"
FT /evidence="ECO:0000305|PubMed:11839312"
FT REGION 375..453
FT /note="Topological domain 4"
FT /evidence="ECO:0000305|PubMed:11839312"
FT ACT_SITE 20
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:23517223"
FT ACT_SITE 108
FT /note="Non-phosphorylated intermediate"
FT /evidence="ECO:0000305|PubMed:11839312,
FT ECO:0000305|PubMed:14725765, ECO:0000305|PubMed:16880541"
FT ACT_SITE 329
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:23517223"
FT BINDING 17
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000269|PubMed:14725765,
FT ECO:0000269|PubMed:18690721, ECO:0007744|PDB:1P5D,
FT ECO:0007744|PDB:3BKQ"
FT BINDING 17
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000269|PubMed:14725765,
FT ECO:0007744|PDB:1PCJ"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000269|PubMed:11839312,
FT ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672,
FT ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721,
FT ECO:0000269|PubMed:23517223"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11839312,
FT ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672,
FT ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721,
FT ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223,
FT ECO:0000269|PubMed:24403075"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11839312,
FT ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672,
FT ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721,
FT ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223,
FT ECO:0000269|PubMed:24403075"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11839312,
FT ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672,
FT ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721,
FT ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223,
FT ECO:0000269|PubMed:24403075"
FT BINDING 285
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000269|PubMed:14725765,
FT ECO:0000269|PubMed:18690721, ECO:0007744|PDB:1P5D,
FT ECO:0007744|PDB:3BKQ"
FT BINDING 308
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000269|PubMed:14725765,
FT ECO:0000269|PubMed:18690721, ECO:0007744|PDB:1P5D,
FT ECO:0007744|PDB:3BKQ"
FT BINDING 308
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000269|PubMed:14725765,
FT ECO:0007744|PDB:1PCJ"
FT BINDING 325..329
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000269|PubMed:14725765,
FT ECO:0000269|PubMed:18690721, ECO:0007744|PDB:1P5D,
FT ECO:0007744|PDB:3BKQ"
FT BINDING 325..329
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000269|PubMed:14725765,
FT ECO:0007744|PDB:1PCJ"
FT BINDING 421..425
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000269|PubMed:14725765,
FT ECO:0000269|PubMed:18690721, ECO:0007744|PDB:1P5D,
FT ECO:0007744|PDB:3BKQ"
FT BINDING 421..425
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000269|PubMed:14725765,
FT ECO:0007744|PDB:1PCJ"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11839312,
FT ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672,
FT ECO:0000269|PubMed:16880541"
FT MUTAGEN 15
FT /note="R->A: KM halves, decreases processivity as
FT dissociation of G1,6P intermediate increases 25-fold."
FT /evidence="ECO:0000269|PubMed:16595672"
FT MUTAGEN 20
FT /note="R->A: No phosphoglucomutase activity."
FT /evidence="ECO:0000269|PubMed:16595672"
FT MUTAGEN 108
FT /note="S->A,V: About 5% activity, still subject to
FT substrate inhibition and requires G1,6P as an activator;
FT phosphorylation occurs at a different site."
FT /evidence="ECO:0000269|PubMed:11716469"
FT MUTAGEN 108
FT /note="S->C: KM for G1P unchanged, kcat decreases 24-fold;
FT G1,6P stimulates reaction by 2-3 orders of magnitude. No
FT stable protein phosphorylation detected, altered ligation
FT of metal residue."
FT /evidence="ECO:0000269|PubMed:22242625"
FT MUTAGEN 110
FT /note="N->A: KM halves, decreases processivity as
FT dissociation of G1,6P intermediate increases 30-fold."
FT /evidence="ECO:0000269|PubMed:16595672"
FT MUTAGEN 247
FT /note="R->A: Small reduction in KM, small increase in
FT dissociation of G1,6P intermediate."
FT /evidence="ECO:0000269|PubMed:16595672"
FT MUTAGEN 262
FT /note="R->A: Increases KM 2-fold, decreases kcat 9-fold for
FT G1P. Alters flexibility of the hinge region."
FT /evidence="ECO:0000269|PubMed:18690721"
FT MUTAGEN 325
FT /note="E->A: Reduces KM and Vmax approximately 2-fold."
FT /evidence="ECO:0000269|PubMed:14725765"
FT MUTAGEN 329
FT /note="H->A: No phosphoglucomutase activity using G1P as
FT substrate, protein is less easily phosphorylated, no
FT significant change in structure."
FT /evidence="ECO:0000269|PubMed:23517223"
FT MUTAGEN 368
FT /note="P->G: Increases KM 2-fold, decreases kcat 6-fold for
FT G1P. Alters flexibility of the hinge region, structure is
FT less compact."
FT /evidence="ECO:0000269|PubMed:18690721"
FT MUTAGEN 421
FT /note="R->C: Loss of phosphomannomutase activity, very low
FT phosphoglucomutase activity."
FT /evidence="ECO:0000269|PubMed:16595672,
FT ECO:0000269|PubMed:1903398"
FT CONFLICT 4
FT /note="A -> V (in Ref. 1; AAA25701)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="G -> R (in Ref. 1; AAA25701)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="T -> P (in Ref. 1; AAA25701)"
FT /evidence="ECO:0000305"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:1P5D"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 29..45
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:1P5D"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1K35"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1K35"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 260..274
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 289..296
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:1P5D"
FT TURN 333..336
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 342..354
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:2H4L"
FT HELIX 360..365
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:1P5D"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 385..395
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 406..413
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 416..422
FT /evidence="ECO:0007829|PDB:1P5D"
FT STRAND 424..437
FT /evidence="ECO:0007829|PDB:1P5D"
FT HELIX 438..455
FT /evidence="ECO:0007829|PDB:1P5D"
SQ SEQUENCE 463 AA; 50296 MW; 35EE59406379FFB8 CRC64;
MSTAKAPTLP ASIFRAYDIR GVVGDTLTAE TAYWIGRAIG SESLARGEPC VAVGRDGRLS
GPELVKQLIQ GLVDCGCQVS DVGMVPTPVL YYAANVLEGK SGVMLTGSHN PPDYNGFKIV
VAGETLANEQ IQALRERIEK NDLASGVGSV EQVDILPRYF KQIRDDIAMA KPMKVVVDCG
NGVAGVIAPQ LIEALGCSVI PLYCEVDGNF PNHHPDPGKP ENLKDLIAKV KAENADLGLA
FDGDGDRVGV VTNTGTIIYP DRLLMLFAKD VVSRNPGADI IFDVKCTRRL IALISGYGGR
PVMWKTGHSL IKKKMKETGA LLAGEMSGHV FFKERWFGFD DGIYSAARLL EILSQDQRDS
EHVFSAFPSD ISTPEINITV TEDSKFAIIE ALQRDAQWGE GNITTLDGVR VDYPKGWGLV
RASNTTPVLV LRFEADTEEE LERIKTVFRN QLKAVDSSLP VPF
