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NRDG_VIBCH
ID   NRDG_VIBCH              Reviewed;         155 AA.
AC   Q9KM76;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Anaerobic ribonucleoside-triphosphate reductase-activating protein {ECO:0000250|UniProtKB:P0A9N8};
DE            EC=1.97.1.- {ECO:0000250|UniProtKB:P0A9N8};
DE   AltName: Full=Class III anaerobic ribonucleotide reductase small component {ECO:0000250|UniProtKB:P0A9N8};
GN   Name=nrdG; OrderedLocusNames=VC_A0512;
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 [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   -!- FUNCTION: Activation of anaerobic ribonucleoside-triphosphate reductase
CC       under anaerobic conditions by generation of an organic free radical,
CC       using S-adenosylmethionine and reduced flavodoxin as cosubstrates to
CC       produce 5'-deoxy-adenosine. {ECO:0000250|UniProtKB:P0A9N8}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-
CC         methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+)
CC         + L-methionine + semiquinone [flavodoxin]; Xref=Rhea:RHEA:61976,
CC         Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:14480, Rhea:RHEA-COMP:15993,
CC         Rhea:RHEA-COMP:15994, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:29947, ChEBI:CHEBI:32722, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:140311;
CC         Evidence={ECO:0000250|UniProtKB:P0A9N8};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P0A9N8};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000250|UniProtKB:P0A9N4};
CC   -!- SUBUNIT: Forms a tetramer composed of two NrdD and two NrdG subunits.
CC       {ECO:0000250|UniProtKB:P0A9N8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9N8}.
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC       {ECO:0000305}.
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DR   EMBL; AE003853; AAF96415.1; -; Genomic_DNA.
DR   PIR; E82452; E82452.
DR   RefSeq; NP_232903.1; NC_002506.1.
DR   RefSeq; WP_001106209.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KM76; -.
DR   SMR; Q9KM76; -.
DR   STRING; 243277.VC_A0512; -.
DR   DNASU; 2612588; -.
DR   EnsemblBacteria; AAF96415; AAF96415; VC_A0512.
DR   GeneID; 57741917; -.
DR   KEGG; vch:VC_A0512; -.
DR   PATRIC; fig|243277.26.peg.3138; -.
DR   eggNOG; COG0602; Bacteria.
DR   HOGENOM; CLU_089926_2_1_6; -.
DR   OMA; NQVIHYL; -.
DR   BioCyc; VCHO:VCA0512-MON; -.
DR   Proteomes; UP000000584; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0043365; F:[formate-C-acetyltransferase]-activating enzyme activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012837; NrdG.
DR   InterPro; IPR034457; Organic_radical-activating.
DR   InterPro; IPR001989; Radical_activat_CS.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30352; PTHR30352; 1.
DR   PANTHER; PTHR30352:SF2; PTHR30352:SF2; 1.
DR   PIRSF; PIRSF000368; NrdG; 1.
DR   SFLD; SFLDF00299; anaerobic_ribonucleoside-triph; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   TIGRFAMs; TIGR02491; NrdG; 1.
DR   PROSITE; PS01087; RADICAL_ACTIVATING; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW   Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..155
FT                   /note="Anaerobic ribonucleoside-triphosphate reductase-
FT                   activating protein"
FT                   /id="PRO_0000200541"
FT   BINDING         26
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         30
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         32..34
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         33
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT   BINDING         74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9N4"
SQ   SEQUENCE   155 AA;  17574 MW;  FCCF61F171C21DE6 CRC64;
     MNYHQYYPID VVNGPGTRCT LFVSGCVHQC KGCYNQSTWS LSSGHRYTQE MEDKIIADLK
     DTRIKRRGLS LSGGDPMHPA NLSAVLQLVQ RVKTECPDKD IWLWTGYTLA ELDDSQQALL
     PYIDVLVDGK FIQEQADPGL EWRGSANQVI HRFTL
 
 
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