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Database: UniProt
Entry: A0A024TR36_9STRA
LinkDB: A0A024TR36_9STRA
Original site: A0A024TR36_9STRA 
ID   A0A024TR36_9STRA        Unreviewed;       297 AA.
AC   A0A024TR36;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating] {ECO:0000256|PIRNR:PIRNR006250};
DE            EC=2.4.2.19 {ECO:0000256|PIRNR:PIRNR006250};
DE   AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000256|PIRNR:PIRNR006250};
GN   ORFNames=H310_10861 {ECO:0000313|EMBL:ETV95812.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV95812.1};
RN   [1] {ECO:0000313|EMBL:ETV95812.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETV95812.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC       {ECO:0000256|PIRNR:PIRNR006250}.
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         Evidence={ECO:0000256|PIRNR:PIRNR006250};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from quinolinate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004893, ECO:0000256|PIRNR:PIRNR006250}.
CC   -!- SUBUNIT: Hexamer formed by 3 homodimers.
CC       {ECO:0000256|PIRNR:PIRNR006250}.
CC   -!- SIMILARITY: Belongs to the NadC/ModD family.
CC       {ECO:0000256|ARBA:ARBA00009400, ECO:0000256|PIRNR:PIRNR006250}.
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DR   EMBL; KI913979; ETV95812.1; -; Genomic_DNA.
DR   RefSeq; XP_008875564.1; XM_008877342.1.
DR   AlphaFoldDB; A0A024TR36; -.
DR   STRING; 157072.A0A024TR36; -.
DR   EnsemblFungi; H310_10861-t26_1; H310_10861-t26_1-p1; H310_10861.
DR   EnsemblProtists; ETV95812; ETV95812; H310_10861.
DR   GeneID; 20087911; -.
DR   VEuPathDB; FungiDB:H310_10861; -.
DR   eggNOG; KOG3008; Eukaryota.
DR   OrthoDB; 5473389at2759; -.
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; 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   ECO:0000256|PIRNR:PIRNR006250};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          31..114
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          116..286
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
SQ   SEQUENCE   297 AA;  31725 MW;  03C0B875D509CB85 CRC64;
     MTFAHLLPPT WKKNVQLWLE DDIPSYDVGG FVVGESNQIA YLLGKSHGVL AGVPFFTAVF
     EAVDCVVEWQ LPEGAMIDPS TVASGKVVVA KVTGKCRNIL LGERTALNIL TRASGIATQA
     AAAVKVARSL GWHGHVAGTR KTTPGFRVVE KYALLVAGAS THRNDLSQMV MLKDNHVWAS
     GSITNAVKRA KTAAGFSMKI EVECRKLEEA VEAATAGADI VMLDNFEPPQ LKQVAATLKQ
     QFPHLLIEAS GGITIDSMGD FVSPHVDIIS QGKLTQGYGA VDFSLKIQKC EGIVAAE
//
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