ID   MANB_KLEPN              Reviewed;         157 AA.
AC   Q48463;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Phosphomannomutase;
DE            Short=PMM;
DE            EC=5.4.2.8;
DE   AltName: Full=ORF17;
DE   Flags: Fragment;
GN   Name=manB; Synonyms=cpsG;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Chedid;
RX   MEDLINE=95204345; PubMed=7896702;
RA   Arakawa Y., Wacharotayankun R., Nagatsuka T., Ito H., Kato N.,
RA   Ohta M.;
RT   "Genomic organization of the Klebsiella pneumoniae cps region
RT   responsible for serotype K2 capsular polysaccharide synthesis in the
RT   virulent strain Chedid.";
RL   J. Bacteriol. 177:1788-1796(1995).
CC   -!- FUNCTION: Involved in the biosynthesis of the K2 capsular
CC       polysaccharide biosynthesis.
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: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
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DR   EMBL; D21242; BAA04788.1; -; Genomic_DNA.
DR   PIR; F56146; F56146.
DR   HSSP; P26276; 1K35.
DR   BRENDA; 5.4.2.8; 758.
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; IPR016066; A-D-PHexomutase_CS.
DR   Gene3D; G3DSA:3.40.120.10; A-D-PHexomutase_a/b/a-I/II/III; 1.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Isomerase;
KW   Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW   Phosphoprotein.
FT   CHAIN         1   >157       Phosphomannomutase.
FT                                /FTId=PRO_0000147820.
FT   ACT_SITE     98     98       Phosphoserine intermediate (By
FT                                similarity).
FT   METAL        98     98       Magnesium; via phosphate group (By
FT                                similarity).
FT   NON_TER     157    157
SQ   SEQUENCE   157 AA;  17234 MW;  6AC0F03089741D95 CRC64;
     MTQLTCFKAY DIRGELGEEL NEDIAYRIGR AYGEFLKPGK IVVGGDVRLT SESLNVALAR
     GLMDAGTDVL DIGLSGTEEI YFATFHLGVD GGIEVTASHN PMNYNGMKLV RENAKPISGD
     TGLRDIQRLA EENQFPPVDP ARRGTLRQIS VLKEYVD
//