ID   MANB_SALMO              Reviewed;         456 AA.
AC   Q01411;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Phosphomannomutase;
DE            Short=PMM;
DE            EC=5.4.2.8;
GN   Name=manB; Synonyms=rfbL;
OS   Salmonella montevideo.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=115981;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M40;
RX   PubMed=1383393; DOI=10.1099/00221287-138-9-1843;
RA   Lee S.J., Romana L.K., Reeves P.R.;
RT   "Sequence and structural analysis of the rfb (O antigen) gene cluster from
RT   a group C1 Salmonella enterica strain.";
RL   J. Gen. Microbiol. 138:1843-1855(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 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   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; M84642; AAB49391.1; -; Genomic_DNA.
DR   RefSeq; WP_044782506.1; NZ_MXWS01000078.1.
DR   AlphaFoldDB; Q01411; -.
DR   SMR; Q01411; -.
DR   UniPathway; UPA00126; UER00424.
DR   UniPathway; UPA00281; -.
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   Isomerase; Lipopolysaccharide biosynthesis; Magnesium; Metal-binding;
KW   Phosphoprotein.
FT   CHAIN           1..456
FT                   /note="Phosphomannomutase"
FT                   /id="PRO_0000147821"
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   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   456 AA;  49900 MW;  F2443A7B6CA83460 CRC64;
     MNNLTCFKAY DIRGRLGEEL NEDIAWRIGR AYGEYLKPKT IVLGGDVRLT SEALKLALAK
     GLQDAGVDVL DIGMSGTEEI YFATFHLGVD GGIEVTASHN PMDYNGMKLV REGARPISGD
     TGLRDVQRLA EAGDFPPVND AARGSYRQIS LRDAYIDHLL AYISVNNLTP LKLVVNSGNG
     AAGPVIDAIE ARLKALGAPV EFIKIHNTPD GTFPNGIPNP LLPECRDDTR KAVIEHGADM
     GIAFDGDFDR CFLFDEKGQF IEGYYIVGLL AEAFLEKHPG AKIIHDPRLT WNTEAVVTAA
     GGTPVMSKTG HAFIKERMRT EDAIYGGEMS AHHYFRDFAY CDSGMIPWLL VAELVCLKGQ
     SLGELVRDRM AAFPASGEIN SRLAEPAAAI ARVEAHFAEE AQAVDRTDGL SMSFADWRFN
     LRSSNTEPVV RLNVESRGDI PLMEARTKEI LQLLNS