位置:首页 > 蛋白库 > NADC_RHORU
NADC_RHORU
ID   NADC_RHORU              Reviewed;         296 AA.
AC   P77938;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Probable nicotinate-nucleotide pyrophosphorylase [carboxylating];
DE            EC=2.4.2.19;
DE   AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating];
DE            Short=QAPRTase;
GN   Name=nadC;
OS   Rhodospirillum rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=1085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UR1;
RX   PubMed=7721706; DOI=10.1128/jb.177.8.2157-2163.1995;
RA   Shelver D., Kerby R.L., He Y., Roberts G.P.;
RT   "Carbon monoxide-induced activation of gene expression in Rhodospirillum
RT   rubrum requires the product of cooA, a member of the cyclic AMP receptor
RT   protein family of transcriptional regulators.";
RL   J. Bacteriol. 177:2157-2163(1995).
CC   -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate;
CC         Xref=Rhea:RHEA:12733, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29959, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC         ChEBI:CHEBI:58017; EC=2.4.2.19;
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from quinolinate: step 1/1.
CC   -!- SUBUNIT: Hexamer formed by 3 homodimers. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U65510; AAC45128.1; -; Genomic_DNA.
DR   PIR; T51326; T51326.
DR   RefSeq; WP_011389186.1; NZ_CP077803.1.
DR   AlphaFoldDB; P77938; -.
DR   SMR; P77938; -.
DR   OMA; DMIMLKD; -.
DR   UniPathway; UPA00253; UER00331.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IMP:CACAO.
DR   CDD; cd01572; QPRTase; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.90.1170.20; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR004393; NadC.
DR   InterPro; IPR027277; NadC/ModD.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR   InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR   InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR   PANTHER; PTHR32179; PTHR32179; 1.
DR   Pfam; PF01729; QRPTase_C; 1.
DR   Pfam; PF02749; QRPTase_N; 1.
DR   PIRSF; PIRSF006250; NadC_ModD; 1.
DR   SUPFAM; SSF51690; SSF51690; 1.
DR   TIGRFAMs; TIGR00078; nadC; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN           1..296
FT                   /note="Probable nicotinate-nucleotide pyrophosphorylase
FT                   [carboxylating]"
FT                   /id="PRO_0000155948"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         140..142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         249..251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         270..272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   296 AA;  30536 MW;  96605A621C84DCAE CRC64;
     MRPNHPVAAL SPFAIDEAVR RALAEDLGRA GDITSTATIP AATRAHARFV ARQPGILAGL
     GCARSAFALL DDTVTFTTPL EDGAEIAAGQ TVAEVAGAAR TILAAERTAL NFLGHLSGIA
     TRTRRFGDAI AHTRARLTCT RKTTPGLRGL EKYAVRCGGG SNHRFGLDDA VLIKDNHIAV
     AGGVSAALSR ARAGVGHMVR IEIEVDTLEQ LAEVLAVGGA EVVLLDNMDA PTLTRAVDMV
     AGRLVTEASG GVSLDTIAAL AESGVDYISV GALTHSVTTL DIGLDIVVAP PKAERA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024