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Database: UniProt
Entry: I3CGT3_9GAMM
LinkDB: I3CGT3_9GAMM
Original site: I3CGT3_9GAMM 
ID   I3CGT3_9GAMM            Unreviewed;       283 AA.
AC   I3CGT3;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=BegalDRAFT_1954 {ECO:0000313|EMBL:EIJ42826.1};
OS   Beggiatoa alba B18LD.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Beggiatoa.
OX   NCBI_TaxID=395493 {ECO:0000313|EMBL:EIJ42826.1, ECO:0000313|Proteomes:UP000005744};
RN   [1] {ECO:0000313|EMBL:EIJ42826.1, ECO:0000313|Proteomes:UP000005744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B18LD {ECO:0000313|EMBL:EIJ42826.1,
RC   ECO:0000313|Proteomes:UP000005744};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Samuel K., Teske A.,
RA   Mueller J., Woyke T.;
RT   "Improved High-Quality Draft sequence of Beggiatoa alba B18lD.";
RL   Submitted (NOV-2011) 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; JH600070; EIJ42826.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3CGT3; -.
DR   STRING; 395493.BegalDRAFT_1954; -.
DR   eggNOG; COG0157; Bacteria.
DR   HOGENOM; CLU_039622_0_3_6; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000005744; 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:UP000005744};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          26..114
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          117..280
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
SQ   SEQUENCE   283 AA;  30539 MW;  C2D5A3B5F7A97DEF CRC64;
     MMNTLTSPAL PADIETVVRM ALAEDVGSGD VTAQLIDAQA QATAQVITRE SAVLCGVAWF
     SEVFRQLDEK VQIQWFAHDG ERVVPDQVLC KLSGASRSLL TGERTALNFL QLLSGTATQT
     ATYVEAVSHT KTKILDTRKT IPVLRTAQKY AVCCGGGMNH RMGLYDAFLI KENHIFAAGS
     IPQALDKART IGKNLLIEIE VENLQELQIA LAAGATRILL DNFSLPMFRE AVQLTQGRAS
     LEASGGVSLE TLQAIAETGV DFISIGGLTK HVQAIDLSMR IID
//
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