ID   RFBK_SALMU              Reviewed;         478 AA.
AC   Q00330;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Phosphomannomutase;
DE            Short=PMM;
DE            EC=5.4.2.8;
GN   Name=manB; Synonyms=rfbK;
OS   Salmonella muenchen.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M67;
RX   PubMed=1379320; DOI=10.1111/j.1365-2958.1992.tb00859.x;
RA   Brown P.K., Romana L.K., Reeves P.R.;
RT   "Molecular analysis of the rfb gene cluster of Salmonella serovar muenchen
RT   (strain M67): the genetic basis of the polymorphism between groups C2 and
RT   B.";
RL   Mol. Microbiol. 6:1385-1394(1992).
CC   -!- FUNCTION: Involved in GDP-mannose biosynthesis which serves as the
CC       activated sugar nucleotide precursor for mannose residues in cell
CC       surface polysaccharides. This enzyme participates in synthesis of the
CC       LPS group C2 O antigen.
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}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; X61917; CAA43916.1; -; Genomic_DNA.
DR   PIR; S22622; S22622.
DR   AlphaFoldDB; Q00330; -.
DR   SMR; Q00330; -.
DR   PRIDE; Q00330; -.
DR   UniPathway; UPA00126; UER00424.
DR   UniPathway; UPA00281; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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   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; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..478
FT                   /note="Phosphomannomutase"
FT                   /id="PRO_0000147825"
FT   TRANSMEM        30..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        111
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  52813 MW;  982E5B885083B893 CRC64;
     MKNIYNTYDV INKSGINFGT SGARGLVTDF TPEVCARFTI SFLTVMQQRF SFTTVALAID
     NRPSSYAMAQ ACAAALQEKG IKTVYYGVIP TPALAHQSIS DKVPAIMVTG SHIPFDRNGL
     KFYRPDGEIT KDDENAIIHV DASFMQPKLE QLTISTIAAR NYILRYTSLF PMPFLKNKRI
     GIYEHSSAGR DLYKTLFKML GATVVSLARS DEFVPIDTEA VSEDDRNKAI TWAKKYQLDA
     IFSTDGDGDR PLIADEYGNW LRGDILGLLC SLELAADAVA IPVSCNSTIS SGNFFKHVER
     TKIGSPYVIA AFAKLSANYN CIAGFEANGG FLLGSDVYIN QRLLKALPTR DALLPAIMLL
     FGSKDKSISE LVKKLPARYT YSNRLQDISV KTSMSLINLG LTDQEDFLQY IGFNKHHILH
     SDVTDGFRIT IDNNNIIHLR PSGNAPELRC YAEADSQEDA CNIVETVLSN IKSKLGRA