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   16-JUN-2009, entry version 69.
DE   RecName: Full=Phosphomannomutase;
DE            Short=PMM;
DE            EC=5.4.2.8;
GN   Name=rfbB; OrderedLocusNames=VC_0242;
OS   Vibrio cholerae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=El Tor O17 / Serotype O1;
RX   MEDLINE=92212870; 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 / Serotype O1;
RX   MEDLINE=20406833; 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.,
RA   Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
RA   Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
RA   Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
RA   Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
RA   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: Alpha-D-mannose 1-phosphate = D-mannose 6-
CC       phosphate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-D-mannose
CC       biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-
CC       phosphate: step 2/2.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane (Probable).
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
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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; -.
DR   HSSP; P26276; 1K2Y.
DR   GeneID; 2614705; -.
DR   GenomeReviews; AE003852_GR; VC_0242.
DR   KEGG; vch:VC0242; -.
DR   TIGR; VC_0242; -.
DR   HOGENOM; Q06951; -.
DR   OMA; Q06951; LENKIFI.
DR   BRENDA; 5.4.2.8; 19019.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:EC.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
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; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; A-D-PHexomutase_N.
DR   Gene3D; G3DSA:3.40.120.10; A-D-PHexomutase_a/b/a-I/II/III; 3.
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   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Isomerase;
KW   Lipopolysaccharide biosynthesis; Magnesium; Membrane; Metal-binding;
KW   Phosphoprotein.
FT   CHAIN         1    463       Phosphomannomutase.
FT                                /FTId=PRO_0000147827.
FT   ACT_SITE    103    103       Phosphoserine intermediate (By
FT                                similarity).
FT   METAL       103    103       Magnesium; via phosphate group (By
FT                                similarity).
FT   METAL       248    248       Magnesium (By similarity).
FT   METAL       250    250       Magnesium (By similarity).
FT   METAL       252    252       Magnesium (By similarity).
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
//