ID RFBB_VIBCH Reviewed; 463 AA. AC Q06951; Q9JQ14; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 133. DE RecName: Full=Phosphomannomutase; DE Short=PMM; DE EC=5.4.2.8; GN Name=rfbB; OrderedLocusNames=VC_0242; OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=243277; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=El Tor O17 / Serotype O1; RX PubMed=1372980; DOI=10.1073/pnas.89.7.2566; RA Stroeher U.H., Karageorgos L.E., Morona R., Manning P.A.; RT "Serotype conversion in Vibrio cholerae O1."; RL Proc. Natl. Acad. Sci. U.S.A. 89:2566-2570(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39315 / El Tor Inaba N16961; RX PubMed=10952301; DOI=10.1038/35020000; RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A., RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.; RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio RT cholerae."; RL Nature 406:477-483(2000). CC -!- FUNCTION: Involved in GDP-mannose biosynthesis which serves as the CC activated sugar nucleotide precursor for mannose residues in cell CC surface polysaccharides. 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X59554; CAA42135.1; -; Genomic_DNA. DR EMBL; AE003852; AAF93418.1; -; Genomic_DNA. DR PIR; S28469; S28469. DR RefSeq; NP_229899.1; NC_002505.1. DR RefSeq; WP_000661577.1; NZ_LT906614.1. DR AlphaFoldDB; Q06951; -. DR SMR; Q06951; -. DR STRING; 243277.VC_0242; -. DR DNASU; 2614705; -. DR EnsemblBacteria; AAF93418; AAF93418; VC_0242. DR KEGG; vch:VC_0242; -. DR PATRIC; fig|243277.26.peg.223; -. DR eggNOG; COG1109; Bacteria. DR HOGENOM; CLU_016950_9_2_6; -. DR UniPathway; UPA00126; UER00424. DR UniPathway; UPA00281; -. DR PHI-base; PHI:703; -. DR Proteomes; UP000000584; Chromosome 1. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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 CDD; cd03089; PMM_PGM; 1. DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3. DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1. 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 PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1. DR PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 1. 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; SSF55957; Phosphoglucomutase, C-terminal domain; 1. DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3. DR PROSITE; PS00710; PGM_PMM; 1. PE 3: Inferred from homology; KW Cell membrane; Isomerase; Lipopolysaccharide biosynthesis; Magnesium; KW Membrane; Metal-binding; Phosphoprotein; Reference proteome. FT CHAIN 1..463 FT /note="Phosphomannomutase" FT /id="PRO_0000147827" FT ACT_SITE 103 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000250" FT BINDING 103 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via phosphate group" 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 BINDING 252 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" SQ SEQUENCE 463 AA; 51838 MW; 7212EA3A64BFC6BE CRC64; MKELTCFKAY DIRGQLGSEL DNEIAYRIGR SYGQFLKSEN DADKTVVVGG DVRLTSEALK QALANGLMDA GINVIDIGVT GTEEIYFATF YLGVDGGIEV TASHNPMDYN GMKLVREGSK PISGDTGLRE IQALAEKNEF MDVEVKGNYK KVSLLPEYVD HLISYITPAK IKPMKLVINS GNGAAGHVID ELEKRFIELS IPLEIIKVHH EEDGNFPNGI PNPLLPECRA DTANAVKEHK ADMGIAFDGD FDRCFLFDEN GDFIEGYYIV GLLAEAFLQK EQGAKIIHDP RLSWNTIDVV TKSGGVPVMS KTGHAFIKER MRKEDAIYGG EMSAHHYFRD FGYCDSGMIP WLLITELLSL APDISLSKLI SAKRFLFPCS GEINFKVKQA KLIMEQVYLH YYENSIHFSA IDGISLEFEG WRFNLRDSNT EPLLRLNVES KQNIALMNDK VEELTKLIKK LDI //