ID   ALGC_PSEPK              Reviewed;         463 AA.
AC   Q88C93;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Phosphomannomutase/phosphoglucomutase;
DE            Short=PMM / PGM;
DE            EC=5.4.2.2;
DE            EC=5.4.2.8;
GN   Name=algC; OrderedLocusNames=PP_5288;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
CC   -!- FUNCTION: The phosphomannomutase activity produces a precursor for
CC       alginate polymerization. The alginate layer causes a mucoid phenotype
CC       and provides a protective barrier against host immune defenses and
CC       antibiotics. Also involved in core-LPS biosynthesis due to its
CC       phosphoglucomutase activity. Essential for biofilm production (By
CC       similarity). {ECO:0000250}.
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;
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
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}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; AE015451; AAN70853.1; -; Genomic_DNA.
DR   RefSeq; NP_747389.1; NC_002947.4.
DR   AlphaFoldDB; Q88C93; -.
DR   SMR; Q88C93; -.
DR   STRING; 160488.PP_5288; -.
DR   EnsemblBacteria; AAN70853; AAN70853; PP_5288.
DR   KEGG; ppu:PP_5288; -.
DR   PATRIC; fig|160488.4.peg.5640; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_9_1_6; -.
DR   OMA; HSGEINF; -.
DR   PhylomeDB; Q88C93; -.
DR   BioCyc; PPUT160488:G1G01-5645-MON; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00126; UER00424.
DR   Proteomes; UP000000556; 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   3: Inferred from homology;
KW   Alginate biosynthesis; Isomerase; Lipopolysaccharide biosynthesis;
KW   Magnesium; Metal-binding; Multifunctional enzyme; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..463
FT                   /note="Phosphomannomutase/phosphoglucomutase"
FT                   /id="PRO_0000147815"
FT   ACT_SITE        108
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            421
FT                   /note="Interacts with the biphosphorylated intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   463 AA;  50272 MW;  EAABA30BE7E926F1 CRC64;
     MAHLVPAALP DSIFRAYDIR GVVGKTLHAE TAYWIGRAIG AQSLAQGEPQ VSVGRDGRLS
     GPMLVEQLIK GLVDAGCNVS DVGLVPTPAL YYAANVLAGK SGVMLTGSHN PSDYNGFKIV
     IAGDTLANEQ IQALLTRLKT NDLTLAQGRV EKVEILDRYF KQIVGDVKLA KKLKVVVDCG
     NGAAGVVAPQ LIEALGCEVI PLFCEVDGNF PNHHPDPGKP ENLEDLIAKV KETGADIGLA
     FDGDGDRVGV VTNTGSIVYP DRLLMLFAQD VLSRNPGAEI IFDVKCTRRL TPLIEQHGGR
     ALMWKTGHSL IKKKMKQTGS LLAGEMSGHI FIKERWYGFD DGIYSAARLL EILSKTEQSA
     ENLFAAFPND ISTPEINIDV TDEGKFSIID ALQRDADWGE ANLTTIDGVR VDYANGWGLV
     RASNTTPVLV LRFEADSDAE LQRIKDVFRT QLLRVEPELQ LPF