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Database: UniProt
Entry: A0A1I0C4E7_9RHOB
LinkDB: A0A1I0C4E7_9RHOB
Original site: A0A1I0C4E7_9RHOB 
ID   A0A1I0C4E7_9RHOB        Unreviewed;       285 AA.
AC   A0A1I0C4E7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN04489858_103168 {ECO:0000313|EMBL:SET14313.1};
OS   Paracoccus homiensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=364199 {ECO:0000313|EMBL:SET14313.1, ECO:0000313|Proteomes:UP000199180};
RN   [1] {ECO:0000313|EMBL:SET14313.1, ECO:0000313|Proteomes:UP000199180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17862 {ECO:0000313|EMBL:SET14313.1,
RC   ECO:0000313|Proteomes:UP000199180};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOHO01000003; SET14313.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0C4E7; -.
DR   STRING; 364199.SAMN04489858_103168; -.
DR   OrthoDB; 9782546at2; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000199180; 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:UP000199180};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          28..116
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          118..284
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         139..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         248..250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         269..271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ   SEQUENCE   285 AA;  30108 MW;  933F8BE6EBF59F0F CRC64;
     MTSPAMPPLP DLILEPLIRM ALAEDLGSYG DITTRTVIPA DITYRAAIRA RQPGIASGMQ
     LAAIAFRLVD PDLSITTLCA DGTPFQAGEV LMQIEGPAAS ILSAERVALN FAGRLCGIAT
     MTASFVARTT GTNTRITCTR KTTPGLRLVE KQAVLHGGGF NHRFSLSDAI LIKDNHIAAA
     GGVRPVLQAV KARASHMIRC EIEVDTLDQL AEVLSETGAD VVLLDNMDTP TLQQAVKMAQ
     GQVVLEASGN MRLDRIAEVA ATGVDYISSG ALTHSATTLD LGLDF
//
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