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 27-MAR-2024, entry version 147. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 99287-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-MONOMER; -. DR UniPathway; UPA00126; UER00424. DR UniPathway; UPA00281; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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 CDD; cd03088; ManB; 1. DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3. DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1. 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; IPR036900; A-D-PHexomutase_C_sf. DR InterPro; IPR016066; A-D-PHexomutase_CS. DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1. DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 1. DR Pfam; PF02878; PGM_PMM_I; 1. DR Pfam; PF02879; PGM_PMM_II; 1. DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1. DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3. 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 //