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   03-AUG-2022, entry version 80.
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; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Chedid;
RX   PubMed=7896702; DOI=10.1128/jb.177.7.1788-1796.1995;
RA   Arakawa Y., Wacharotayankun R., Nagatsuka T., Ito H., Kato N., Ohta M.;
RT   "Genomic organization of the Klebsiella pneumoniae cps region responsible
RT   for serotype K2 capsular polysaccharide synthesis in the virulent strain
RT   Chedid.";
RL   J. Bacteriol. 177:1788-1796(1995).
CC   -!- FUNCTION: Involved in the biosynthesis of the K2 capsular
CC       polysaccharide biosynthesis.
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: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; D21242; BAA04788.1; -; Genomic_DNA.
DR   PIR; F56146; F56146.
DR   AlphaFoldDB; Q48463; -.
DR   SMR; Q48463; -.
DR   UniPathway; UPA00126; UER00424.
DR   UniPathway; UPA00934; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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   Pfam; PF02878; PGM_PMM_I; 1.
DR   SUPFAM; SSF53738; SSF53738; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Isomerase; Lipopolysaccharide biosynthesis;
KW   Magnesium; Metal-binding; Phosphoprotein.
FT   CHAIN           1..>157
FT                   /note="Phosphomannomutase"
FT                   /id="PRO_0000147820"
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   NON_TER         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