ID   ALGC_PSESM              Reviewed;         465 AA.
AC   Q88BD4;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=PSPTO_0083;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO53637.1; -; Genomic_DNA.
DR   RefSeq; NP_789942.1; NC_004578.1.
DR   AlphaFoldDB; Q88BD4; -.
DR   SMR; Q88BD4; -.
DR   STRING; 223283.PSPTO_0083; -.
DR   PRIDE; Q88BD4; -.
DR   EnsemblBacteria; AAO53637; AAO53637; PSPTO_0083.
DR   KEGG; pst:PSPTO_0083; -.
DR   PATRIC; fig|223283.9.peg.87; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_9_1_6; -.
DR   OMA; HSGEINF; -.
DR   OrthoDB; 256504at2; -.
DR   PhylomeDB; Q88BD4; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00126; UER00424.
DR   Proteomes; UP000002515; 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; ISS:JCVI.
DR   GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; ISS:JCVI.
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..465
FT                   /note="Phosphomannomutase/phosphoglucomutase"
FT                   /id="PRO_0000147816"
FT   ACT_SITE        110
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
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         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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   BINDING         331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            423
FT                   /note="Interacts with the biphosphorylated intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   465 AA;  50692 MW;  A078D8A974111C2C CRC64;
     MNSPASVAPI LPDTIFRAYD IRGVVEDTLN AETAYWIGRA IGSESLAQNE PNVSVGRDGR
     LSGPELVQQL IQGLHDSGCH VSDVGLVPTP ALYYAANVLA GKTGVMLTGS HNPKDYNGFK
     IVIAGDTLAN EQIQALHERI KTNNLTSQKG SITQVNILDR YFKQIKDDIV MARKLKVVVD
     CGNGAAGVIA PQLIEALGCE VISLFAEVDG NFPNHHPDPG KLENLQDLIA KVKETGADLG
     LAFDGDGDRV GVVTNAGNVV YPDRLLMLFA LDVLKRNPGA DIIFDVKCTR RLTPLISEHG
     GRPVMWKTGH SLIKKEMKKS GALLAGEMSG HIFFKERWFG FDDGIYSAAR LLEILSQEPA
     NAEDLFETFP NDISTPEINI KVTDVTKFSI IEALEKDAQW GDAKLTTIDG VRVDYPKGWG
     LVRASNTTPV LVLRFEAETQ AELERIQGVF HAELKKVAPD LDLPF