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RFBA_VIBCH
ID   RFBA_VIBCH              Reviewed;         465 AA.
AC   Q07024; Q9KVA6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Putative mannose-1-phosphate guanylyltransferase;
DE            EC=2.7.7.13;
DE   AltName: Full=GDP-mannose pyrophosphorylase;
DE            Short=GMP;
DE            Short=GMPP;
GN   Name=rfbA; OrderedLocusNames=VC_0241;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=El Tor O17 / Serotype O1;
RX   PubMed=1372980; DOI=10.1073/pnas.89.7.2566;
RA   Stroeher U.H., Karageorgos L.E., Morona R., Manning P.A.;
RT   "Serotype conversion in Vibrio cholerae O1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2566-2570(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA42134.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X59554; CAA42134.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AE003852; AAF93417.1; -; Genomic_DNA.
DR   PIR; H82345; H82345.
DR   PIR; S28468; S28468.
DR   RefSeq; WP_001894734.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q07024; -.
DR   SMR; Q07024; -.
DR   STRING; 243277.VC_0241; -.
DR   DNASU; 2614704; -.
DR   EnsemblBacteria; AAF93417; AAF93417; VC_0241.
DR   GeneID; 57738977; -.
DR   KEGG; vch:VC_0241; -.
DR   eggNOG; COG0662; Bacteria.
DR   eggNOG; COG0836; Bacteria.
DR   HOGENOM; CLU_035527_1_0_6; -.
DR   OMA; LIVCNEK; -.
DR   BioCyc; VCHO:VC0241-MON; -.
DR   UniPathway; UPA00126; UER00930.
DR   UniPathway; UPA00281; -.
DR   Proteomes; UP000000584; Chromosome 1.
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   3: Inferred from homology;
KW   GTP-binding; Lipopolysaccharide biosynthesis; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..465
FT                   /note="Putative mannose-1-phosphate guanylyltransferase"
FT                   /id="PRO_0000194262"
SQ   SEQUENCE   465 AA;  51916 MW;  7274A5A876F49268 CRC64;
     MFIPVIMAGG SGSRLWPLSR SAFPKQFLSL DSSSQHTMLQ ATIERLQGLP IAEPIVISNE
     DHRFIVAEQI RRYGKKSRII LEPAGRNTAP AIALAAFTAI EQEDDPVLLV LAADHFVKNK
     SAFQAAISQA AQQAEAGKLA TFGIVPTTPE TGYGYIHRGE EVTQGTYEIN SFVEKPQLNI
     AEQYLASGEY YWNSGCFMFK ASVFLNELKQ HSPEIYRQCE LAMQGLSHDY DFIRVGVEEF
     LKCPDDSIDY AVMEHTKLGV VVSMDAGWSD VGSWSALWEV SDKDADGNVC QGDAILSGTS
     NCYIYAPNKL VAAVGLKDIV VVETKDAVLV ADKNQVQEVK KIVEHLKAEN RAEYREHRER
     YRPWGKSDAI DKGERYKVNR ITVEPGKKQS LQMHYHRAEH WVVVSGTAKV TCEGNVKVIT
     ENQSLYIPIG TNHMIENPGK IPLELIEIQS GSYLNEDDVV RFEDK
 
 
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