RFBB_VIBCH
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 03-AUG-2022, entry version 127.
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; Proteobacteria; 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}.
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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 GeneID; 57738978; -.
DR KEGG; vch:VC_0242; -.
DR PATRIC; fig|243277.26.peg.223; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_9_2_6; -.
DR OMA; KCSQVMY; -.
DR BioCyc; VCHO:VC0242-MON; -.
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 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 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
