ID   RFBK7_ECOLX             Reviewed;         453 AA.
AC   P37742;
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   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O7:K1 / VW187;
RX   PubMed=7677991; DOI=10.1128/jb.175.1.148-158.1993;
RA   Marolda C.L., Valvano M.A.;
RT   "Identification, expression, and DNA sequence of the GDP-mannose
RT   biosynthesis genes encoded by the O7 rfb gene cluster of strain VW187
RT   (Escherichia coli O7:K1).";
RL   J. Bacteriol. 175:148-158(1993).
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 O7 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; AF125322; AAC27539.1; ALT_SEQ; Genomic_DNA.
DR   PIR; D40630; D40630.
DR   AlphaFoldDB; P37742; -.
DR   SMR; P37742; -.
DR   STRING; 585034.ECIAI1_2123; -.
DR   eggNOG; COG1109; Bacteria.
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; 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   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..453
FT                   /note="Phosphomannomutase"
FT                   /id="PRO_0000147823"
FT   ACT_SITE        96
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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"
SQ   SEQUENCE   453 AA;  49932 MW;  F1D1F69F97804391 CRC64;
     MLTCFKAYDI RGKLGEELNE DIAWRIGRAY GEFLKPKTIV LGGDVRLTSE TLKLALAKGL
     QDAGVDVLDI GMSGTEEIYF ATFHLGVDGG IEVTASHNPM DYNGMKLVRE GARPISGDTG
     LRDVQRLAEA NDFPPVDETK RGRYQQINLR DAYVDHLFGY INVKNLTPLK LVINSGNGAA
     GPVVDAIEAR FKALGAPVEL IKVHNTPDGN FPNGIPNPLL PECRDDTRNA VIKHGADMGI
     AFDGDFDRCF LFDEKGQFIE GYYIVGLLAE AFLEKNPGAK IIHDPRLSWN TVDVVTAAGT
     PVMSKTGHAF IKERMRKEDA IYGGEMSAHH YFRDFAYCDT GMIPWLLVAE LVCLKGKTLG
     ELVRDRMAAF PASGEINSKL AHPVEAINRV EQHFSRDAGG GSHRWHQHDL CRLAALTCAS
     SNTEPVVRLN VESRGDVPLM EEKTKLILEL LNK