RFBM_SALMU
ID RFBM_SALMU Reviewed; 473 AA.
AC Q00473;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Mannose-1-phosphate guanylyltransferase;
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;
OS Salmonella muenchen.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=596;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M67;
RX PubMed=1379320; DOI=10.1111/j.1365-2958.1992.tb00859.x;
RA Brown P.K., Romana L.K., Reeves P.R.;
RT "Molecular analysis of the rfb gene cluster of Salmonella serovar muenchen
RT (strain M67): the genetic basis of the polymorphism between groups C2 and
RT B.";
RL Mol. Microbiol. 6:1385-1394(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 group C2 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 -!- 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:0000250}.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.
CC {ECO:0000305}.
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DR EMBL; X61917; CAA43915.1; -; Genomic_DNA.
DR RefSeq; WP_000040079.1; NZ_VUJE01000001.1.
DR AlphaFoldDB; Q00473; -.
DR SMR; Q00473; -.
DR PATRIC; fig|596.10.peg.4303; -.
DR UniPathway; UPA00126; UER00930.
DR UniPathway; UPA00281; -.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase 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 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 3: Inferred from homology;
KW GTP-binding; Lipopolysaccharide biosynthesis; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..473
FT /note="Mannose-1-phosphate guanylyltransferase"
FT /id="PRO_0000194260"
SQ SEQUENCE 473 AA; 52927 MW; B90AD7D445E2100B CRC64;
MSKLIPVIMA GGIGSRLWPL SREEHPKQFL SVDGELSMLQ NTIKRLTPLL AGEPLVICND
SHRFLVAEQL RAINKLANNI ILEPVGRNTA PAIALAAFCS LQNVVDEDPL LLVLAADHVI
RDEKVFLKAI NHAEFFATQG KLVTFGIVPT QAETGYGYIC RGEAIGEDAF SVAEFVEKPD
FDTARHYVES EKYYWNSGMF LFRASSYLQE LKDLSPDIYQ ACENAVGSIN PDLDFIRIDK
EAFAMCPSDS IDYAVMEHTR HAVVVPMNAG WSDVGSWSSL WDISKKDPQR NVLHGDIFAY
NSKDNYIYSE KSFISTIGVN NLVIVQTADA LLVSDKDSVQ DVKKVVDYLK ANNRNEHKKH
LEVFRPWGKF SVIHSGDNYL VKRITVKPGA KFAAQMHLHR AEHWIVVSGT ACITKGEEIF
TISENESTFI PANTVHTLKN PATIPLELIE IQSGTYLAED DIIRLEKHSG YLE
