ID   RFBK9_ECOLX             Reviewed;         456 AA.
AC   P37755; P82275;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Phosphomannomutase;
DE            Short=PMM;
DE            EC=5.4.2.8;
GN   Name=manB; Synonyms=rfbK, rfbK2;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O9:K30:H12 / E69;
RX   PubMed=7515042; DOI=10.1128/jb.176.11.3126-3139.1994;
RA   Jayaratne P., Bronner D., Maclachlan R.P., Dodgson C., Kido N.,
RA   Whitfield C.;
RT   "Cloning and analysis of duplicated rfbM and rfbK genes involved in the
RT   formation of GDP-mannose in Escherichia coli O9:K30 and participation of
RT   rfb genes in the synthesis of the group I K30 capsular polysaccharide.";
RL   J. Bacteriol. 176:3126-3139(1994).
RN   [2]
RP   GENE NAME.
RX   PubMed=9004408; DOI=10.1016/s0966-842x(97)82912-5;
RA   Reeves P.R., Hobbs M., Valvano M.A., Skurnik M., Whitfield C., Coplin D.,
RA   Kido N., Klena J., Maskell D., Raetz C.R.H., Rick P.D.;
RT   "Bacterial polysaccharide synthesis and gene nomenclature.";
RL   Trends Microbiol. 4:495-503(1996).
CC   -!- FUNCTION: Involved in GDP-mannose biosynthesis which serves as the
CC       activated sugar nucleotide precursor for mannose residues in cell
CC       surface polysaccharides. This enzyme participates in synthesis of the
CC       LPS O9 antigen.
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   -!- 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; LPS O-antigen
CC       biosynthesis.
CC   -!- MISCELLANEOUS: There are two duplicated genes for manB and manC in this
CC       E.coli strain.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; L27646; AAA21138.1; -; Genomic_DNA.
DR   EMBL; L27632; AAA21140.1; -; Genomic_DNA.
DR   RefSeq; WP_032248255.1; NZ_VKJG01000247.1.
DR   AlphaFoldDB; P37755; -.
DR   SMR; P37755; -.
DR   STRING; 585034.ECIAI1_2103; -.
DR   PRIDE; P37755; -.
DR   UniPathway; UPA00126; UER00424.
DR   UniPathway; UPA00281; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009243; P:O antigen 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   Isomerase; Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW   Phosphoprotein.
FT   CHAIN           1..456
FT                   /note="Phosphomannomutase"
FT                   /id="PRO_0000147824"
FT   ACT_SITE        98
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
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         250
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   VARIANT         392
FT                   /note="A -> R"
FT   VARIANT         441
FT                   /note="T -> V"
FT   VARIANT         446
FT                   /note="A -> E"
FT   VARIANT         449..453
FT                   /note="EEILA -> TELLN"
FT   VARIANT         456
FT                   /note="K -> KEELL"
SQ   SEQUENCE   456 AA;  50423 MW;  40100B6075791BF3 CRC64;
     MTQLTCFKAY DIRGELGEEL NEDIAYRIGR AYGEFLKPGK IVVGGDVRLT SESLKLALAR
     GLMDAGTDVL DIGLSGTEEI YFATFHLGVD GGIEVTASHN PMNYNGMKLV RENAKPISGD
     TGLRDIQRLA EENQFPPVDP ARRGTLRQIS VLKEYVDHLM GYVDLANFTR PLKLVVNSGN
     GAAGHVIDEV EKRFAAAGVP VTFIKVHHQP DGHFPNGIPN PLLPECRQDT ADAVREHQAD
     MGIAFDGDFD RCFLFDDEAS FIEGYYIVGL LAEAFLQKQP GAKIIHDPRL TWNTVDIVTR
     NGGQPVMSKT GHAFIKERMR QEDAIYGGEM SAHHYFRDFA YCDSGMIPWL LVAELLCLKN
     SSLKSLVADR QAAFPASGEI NRKLGNAAEA IARIRAQYEP AAAHIDTTDG ISIEYPEWRF
     NLRTSNTEPV VRLNVESRAD TALMNAKTEE ILALLK