RFBM_SALTY
ID RFBM_SALTY Reviewed; 479 AA.
AC P26404;
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=Mannose-1-phosphate guanylyltransferase RfbM;
DE EC=2.7.7.13;
DE AltName: Full=GDP-mannose pyrophosphorylase;
DE Short=GMP;
DE Short=GMPP;
DE AltName: Full=GTP--mannose-1-phosphate guanylyltransferase;
GN Name=rfbM; OrderedLocusNames=STM2084;
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).
RN [3]
RP PROTEIN SEQUENCE OF 1-13, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=LT2;
RX PubMed=8922954; DOI=10.1093/glycob/6.6.591;
RA Elling L., Ritter J.E., Verseck S.;
RT "Expression, purification and characterization of recombinant
RT phosphomannomutase and GDP-alpha-D-mannose pyrophosphorylase from
RT Salmonella enterica, group B, for the synthesis of GDP-alpha-D-mannose from
RT D-mannose.";
RL Glycobiology 6:591-597(1996).
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 + GTP + H(+) = diphosphate + GDP-
CC alpha-D-mannose; Xref=Rhea:RHEA:15229, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:58409; EC=2.7.7.13;
CC Evidence={ECO:0000269|PubMed:8922954};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.01 mM for mannose-1-phosphate {ECO:0000269|PubMed:8922954};
CC KM=0.20 mM for GTP {ECO:0000269|PubMed:8922954};
CC Vmax=1.80 umol/min/mg enzyme toward mannose-1-phosphate
CC {ECO:0000269|PubMed:8922954};
CC Vmax=2.40 umol/min/mg enzyme toward GTP {ECO:0000269|PubMed:8922954};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP
CC route): step 1/1.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8922954}.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.
CC {ECO:0000305}.
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DR EMBL; X56793; CAA40128.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20988.1; -; Genomic_DNA.
DR PIR; S15312; S15312.
DR RefSeq; NP_461029.1; NC_003197.2.
DR RefSeq; WP_000009017.1; NC_003197.2.
DR AlphaFoldDB; P26404; -.
DR SMR; P26404; -.
DR STRING; 99287.STM2084; -.
DR PaxDb; P26404; -.
DR PRIDE; P26404; -.
DR EnsemblBacteria; AAL20988; AAL20988; STM2084.
DR GeneID; 1253605; -.
DR KEGG; stm:STM2084; -.
DR PATRIC; fig|99287.12.peg.2206; -.
DR HOGENOM; CLU_035527_1_0_6; -.
DR OMA; IACVGMK; -.
DR PhylomeDB; P26404; -.
DR BioCyc; SENT99287:STM2084-MON; -.
DR SABIO-RK; P26404; -.
DR UniPathway; UPA00126; UER00930.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; IBA:GO_Central.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.10; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR006375; Man1P_GuaTrfase/Man6P_Isoase.
DR InterPro; IPR001538; Man6P_isomerase-2_C.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF01050; MannoseP_isomer; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR01479; GMP_PMI; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; GTP-binding; Lipopolysaccharide biosynthesis;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..479
FT /note="Mannose-1-phosphate guanylyltransferase RfbM"
FT /id="PRO_0000194261"
SQ SEQUENCE 479 AA; 54046 MW; FE9E84D5CEE1F118 CRC64;
MSFLPVIMAG GTGSRLWPLS REYHPKQFLS VEGKLSMLQN TIKRLASLST EEPVVICNDR
HRFLVAEQLR EIDKLANNII LEPVGRNTAP AIALAAFCAL QNADNADPLL LVLAADHVIQ
DEIAFTKAVR HAEEYAANGK LVTFGIVPTH AETGYGYIRR GELIGNDAYA VAEFVEKPDI
DTAGDYFKSG KYYWNSGMFL FRASSYLNEL KYLSPEIYKA CEKAVGHINP DLDFIRIDKE
EFMSCPSDSI DYAVMEHTQH AVVIPMSAGW SDVGSWSSLW DISNKDHQRN VLKGDIFAHA
CNDNYIYSED MFISAIGVSN LVIVQTTDAL LVANKDTVQD VKKIVDYLKR NDRNEYKQHQ
EVFRPWGKYN VIDSGKNYLV RCITVKPGEK FVAQMHHHRA EHWIVLSGTA RVTKGEQTYM
VSENESTFIP PNTIHALENP GMTPLKLIEI QSGTYLGEDD IIRLEQRSGF SKEWTNERS
