RFBK_SALTY
ID RFBK_SALTY Reviewed; 477 AA.
AC P26405;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Phosphomannomutase;
DE Short=PMM;
DE EC=5.4.2.8;
GN Name=rfbK; OrderedLocusNames=STM2083;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=1710759; DOI=10.1111/j.1365-2958.1991.tb00741.x;
RA Jiang X.-M., Neal B., Santiago F., Lee S.J., Romana L.K., Reeves P.R.;
RT "Structure and sequence of the rfb (O antigen) gene cluster of Salmonella
RT serovar typhimurium (strain LT2).";
RL Mol. Microbiol. 5:695-713(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 B 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; X56793; CAA40129.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20987.1; -; Genomic_DNA.
DR PIR; S15313; S15313.
DR RefSeq; NP_461028.1; NC_003197.2.
DR RefSeq; WP_001103643.1; NC_003197.2.
DR AlphaFoldDB; P26405; -.
DR SMR; P26405; -.
DR STRING; 99287.STM2083; -.
DR PaxDb; P26405; -.
DR EnsemblBacteria; AAL20987; AAL20987; STM2083.
DR GeneID; 1253604; -.
DR KEGG; stm:STM2083; -.
DR PATRIC; fig|99287.12.peg.2205; -.
DR HOGENOM; CLU_045514_1_0_6; -.
DR OMA; VPVSCNT; -.
DR PhylomeDB; P26405; -.
DR BioCyc; SENT99287:STM2083-MON; -.
DR UniPathway; UPA00126; UER00424.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0008966; F:phosphoglucosamine mutase activity; IBA:GO_Central.
DR GO; GO:0004615; F:phosphomannomutase activity; IBA:GO_Central.
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 GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
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; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..477
FT /note="Phosphomannomutase"
FT /id="PRO_0000147826"
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 477 AA; 52086 MW; BA6BF851AB931915 CRC64;
MNVVNNSRDV IYSSGIVFGT SGARGLVKDF TPQVCAAFTV SFVAVMQEHF SFDTVALAID
NRPSSYGMAQ ACAAALADKG VNCIFYGVVP TPALAFQSMS DNMPAIMVTG SHIPFERNGL
KFYRPDGEIT KHDEAAILSV EDTCSHLELK ELIVSEMAAV NYISRYTSLF STPFLKNKRI
GIYEHSSAGR DLYKPLFIAL GAEVVSLGRS DNFVPIDTEA VSKEDREKAR SWAKEFDLDA
IFSTDGDGDR PLIADEAGEW LRGDILGLLC SLALDAEAVA IPVSCNSIIS SGRFFKHVKL
TKIGSPYVIE AFNELSRSYS RIVGFEANGG FLLGSDICIN EQNLHALPTR DAVLPAIMLL
YKSRNTSISA LVNELPTRYT HSDRLQGITT DKSQSLISMG RENLSNLLSY IGLENEGAIS
TDMTDGMRIT LRDGCIVHLR ASGNAPELRC YAEANLLNRA QDLVNTTLAN IKKRCLL
