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Database: UniProt
Entry: I4ZAI5_9BACT
LinkDB: I4ZAI5_9BACT
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ID   I4ZAI5_9BACT            Unreviewed;       284 AA.
AC   I4ZAI5;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=nicotinate-nucleotide diphosphorylase (carboxylating) {ECO:0000256|ARBA:ARBA00011944};
DE            EC=2.4.2.19 {ECO:0000256|ARBA:ARBA00011944};
DE   AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000256|ARBA:ARBA00033102};
GN   ORFNames=PrebiDRAFT_1526 {ECO:0000313|EMBL:EIM33227.1};
OS   Prevotella bivia DSM 20514.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=868129 {ECO:0000313|EMBL:EIM33227.1, ECO:0000313|Proteomes:UP000002786};
RN   [1] {ECO:0000313|EMBL:EIM33227.1, ECO:0000313|Proteomes:UP000002786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20514 {ECO:0000313|EMBL:EIM33227.1,
RC   ECO:0000313|Proteomes:UP000002786};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Munk A.C.C., Kyrpides N., Mavromatis K.,
RA   Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "Improved High-Quality Draft genome of Prevotella bivia DSM 20514.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC       {ECO:0000256|ARBA:ARBA00003237}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from quinolinate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004893}.
CC   -!- SIMILARITY: Belongs to the NadC/ModD family.
CC       {ECO:0000256|ARBA:ARBA00009400, ECO:0000256|PIRNR:PIRNR006250}.
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DR   EMBL; JH660660; EIM33227.1; -; Genomic_DNA.
DR   RefSeq; WP_004338013.1; NZ_JH660660.1.
DR   AlphaFoldDB; I4ZAI5; -.
DR   GeneID; 78531480; -.
DR   HOGENOM; CLU_039622_0_1_10; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000002786; Unassembled WGS sequence.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01572; QPRTase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.90.1170.20; Quinolinate phosphoribosyl transferase, N-terminal domain; 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   NCBIfam; TIGR00078; nadC; 1.
DR   PANTHER; PTHR32179; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE [CARBOXYLATING]; 1.
DR   PANTHER; PTHR32179:SF3; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE [CARBOXYLATING]; 1.
DR   Pfam; PF01729; QRPTase_C; 1.
DR   Pfam; PF02749; QRPTase_N; 1.
DR   PIRSF; PIRSF006250; NadC_ModD; 1.
DR   SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR   SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|PIRNR:PIRNR006250};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002786};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          20..109
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          111..281
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
SQ   SEQUENCE   284 AA;  31240 MW;  A366E897EED21A3C CRC64;
     MISVEALNDR LIDLAFSEDI GDGDHTTLCC IPADEIGKSK LLIKEKGIVA GVAIAKKIFA
     RFDDTLKVTT LIEDGTPVMP GDIVMTVEGC VQSLLQTERL MLNVMQRMSG IATMTHRYQQ
     ALIDAGTKTR VLDTRKTTPG MRMLEKEAVK IGGGMNHRIG LFDMILLKDN HVDFCGGIHN
     AISRAKAYCK EKGKDLKIEC EVRNFKELEE ALAEGCDRIM FDNFTPEDTL KAVKIVDGRC
     ETESSGGITF DTMIPYAKAG VDFISFGALT HSCKGLDMSF KAME
//
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