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FBID_COLP3
ID   FBID_COLP3              Reviewed;         210 AA.
AC   Q47WW8;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=3-phospho-D-glycerate guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE            Short=3PG guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE            EC=2.7.7.106 {ECO:0000255|HAMAP-Rule:MF_02114};
GN   Name=fbiD {ECO:0000255|HAMAP-Rule:MF_02114}; OrderedLocusNames=CPS_4046;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681;
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC   -!- FUNCTION: Guanylyltransferase that catalyzes the activation of (2R)-3-
CC       phosphoglycerate (3PG) as 3-[(R)-glyceryl]-diphospho-5'-guanosine, via
CC       the condensation of 3PG with GTP. It is involved in the biosynthesis of
CC       a derivative of the hydride carrier cofactor coenzyme F420, 3PG-F420.
CC       {ECO:0000255|HAMAP-Rule:MF_02114}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + GTP + H(+) = 3-[(R)-glyceryl]-
CC         diphospho-5'-guanosine + diphosphate; Xref=Rhea:RHEA:63440,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:58272, ChEBI:CHEBI:147306; EC=2.7.7.106;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02114};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02114}.
CC   -!- SIMILARITY: Belongs to the CofC family. {ECO:0000255|HAMAP-
CC       Rule:MF_02114}.
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DR   EMBL; CP000083; AAZ28067.1; -; Genomic_DNA.
DR   RefSeq; WP_011044784.1; NC_003910.7.
DR   AlphaFoldDB; Q47WW8; -.
DR   SMR; Q47WW8; -.
DR   STRING; 167879.CPS_4046; -.
DR   DNASU; 3522326; -.
DR   EnsemblBacteria; AAZ28067; AAZ28067; CPS_4046.
DR   KEGG; cps:CPS_4046; -.
DR   HOGENOM; CLU_076569_1_0_6; -.
DR   OMA; HYDEDSY; -.
DR   OrthoDB; 1930370at2; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000000547; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043814; F:phospholactate guanylyltransferase activity; IEA:InterPro.
DR   GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_02114; CofC; 1.
DR   InterPro; IPR002835; CofC.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR40392; PTHR40392; 1.
DR   Pfam; PF01983; CofC; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03552; F420_cofC; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..210
FT                   /note="3-phospho-D-glycerate guanylyltransferase"
FT                   /id="PRO_0000398682"
SQ   SEQUENCE   210 AA;  23486 MW;  86036E25C0B04436 CRC64;
     MRTNIVIPMK DPQLSKTRLD PQLSSRQRQA LALSMFKTTL SFFNKYFPQH HLLVVTASEF
     ISDIACTYGA SVLIETKLGL RQAVESAARW SLNNDFQSQL LIPADIAELD YREFERLLMI
     YRPVPSVLLC PAFDLGTNAL LTTPPNAIPF LYGIDSSLAH QRVAQERDIV CQVIKLPALA
     LDIDTPDDLE LLALLSSPVT QELNKLCKTA
 
 
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