ALGC_PSEAB
ID ALGC_PSEAB Reviewed; 463 AA.
AC Q02E40;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Phosphomannomutase/phosphoglucomutase;
DE Short=PMM / PGM;
DE EC=5.4.2.2 {ECO:0000250|UniProtKB:P26276};
DE EC=5.4.2.8 {ECO:0000250|UniProtKB:P26276};
GN Name=algC; OrderedLocusNames=PA14_70270;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, AND PHOSPHORYLATION AT
RP SER-108.
RC STRAIN=UCBPP-PA14;
RX PubMed=25096199; DOI=10.1007/s00216-014-8045-8;
RA Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT "Potential of liquid-isoelectric-focusing protein fractionation to improve
RT phosphoprotein characterization of Pseudomonas aeruginosa PA14.";
RL Anal. Bioanal. Chem. 406:6297-6309(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. Required for
CC biofilm production. The reaction proceeds via 2 processive phosphoryl
CC transferase reactions; first from enzyme-phospho-Ser-108 to the
CC substrate (generating a bisphosphorylated substrate intermediate and a
CC dephosphorylated enzyme), a 180 degree rotation of the intermediate
CC (probably aided by movement of domain 4), and subsequent transfer of
CC phosphate back to the enzyme. {ECO:0000250|UniProtKB:P26276}.
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:0000250|UniProtKB:P26276};
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:0000250|UniProtKB:P26276};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P26276};
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:0000250|UniProtKB:P26276}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABJ14705.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000438; ABJ14705.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q02E40; -.
DR BMRB; Q02E40; -.
DR SMR; Q02E40; -.
DR iPTMnet; Q02E40; -.
DR PRIDE; Q02E40; -.
DR EnsemblBacteria; ABJ14705; ABJ14705; PA14_70270.
DR KEGG; pau:PA14_70270; -.
DR HOGENOM; CLU_013562_0_1_6; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00126; UER00424.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
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 Alginate biosynthesis; Isomerase; Lipopolysaccharide biosynthesis;
KW Magnesium; Metal-binding; Multifunctional enzyme; Phosphoprotein;
KW Virulence.
FT CHAIN 1..463
FT /note="Phosphomannomutase/phosphoglucomutase"
FT /id="PRO_0000431531"
FT ACT_SITE 108
FT /note="Non-phosphorylated intermediate"
FT /evidence="ECO:0000269|PubMed:25096199"
FT BINDING 17
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 17
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 285
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 308
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 308
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 325..329
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 325..329
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 421..425
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 421..425
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25096199"
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
