NADC_DICDI
ID NADC_DICDI Reviewed; 300 AA.
AC Q75JX0; Q559P0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating];
DE EC=2.4.2.19;
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating];
DE Short=QAPRTase;
GN Name=qprt; ORFNames=DDB_G0272462;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC {ECO:0000250|UniProtKB:Q15274}.
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:0000250|UniProtKB:Q15274};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC {ECO:0000250|UniProtKB:Q15274}.
CC -!- SUBUNIT: Hexamer formed by 3 homodimers.
CC {ECO:0000250|UniProtKB:Q15274}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR EMBL; AAFI02000008; EAL71383.1; -; Genomic_DNA.
DR RefSeq; XP_645294.1; XM_640202.1.
DR AlphaFoldDB; Q75JX0; -.
DR SMR; Q75JX0; -.
DR STRING; 44689.DDB0231362; -.
DR PaxDb; Q75JX0; -.
DR EnsemblProtists; EAL71383; EAL71383; DDB_G0272462.
DR GeneID; 8618460; -.
DR KEGG; ddi:DDB_G0272462; -.
DR dictyBase; DDB_G0272462; qprt.
DR eggNOG; KOG3008; Eukaryota.
DR HOGENOM; CLU_039622_1_0_1; -.
DR InParanoid; Q75JX0; -.
DR OMA; DMIMLKD; -.
DR PhylomeDB; Q75JX0; -.
DR Reactome; R-DDI-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; UER00331.
DR PRO; PR:Q75JX0; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; ISS:dictyBase.
DR GO; GO:0009435; P:NAD biosynthetic process; ISS:dictyBase.
DR GO; GO:0034213; P:quinolinate catabolic process; IBA:GO_Central.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..300
FT /note="Nicotinate-nucleotide pyrophosphorylase
FT [carboxylating]"
FT /id="PRO_0000327816"
FT REGION 5..9
FT /note="Important for hexamer formation"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 107
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 150..151
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 172..173
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 183
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 213
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 234
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 260..262
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 282
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
SQ SEQUENCE 300 AA; 33275 MW; B3FA2F8ADB5C8CAC CRC64;
MEISQLLPKF KIEKIIKEWL EEDIPSFDYG GCVVGSDEKV AHLLGKQNGV FSGSIFFQEI
FNQLGCKVIW FIKDGESFSM THGPEKNKPQ VLAHVIGPVR NILIGERLSL NILSRSCGIT
TQGYNVKKLV DGDNEQQQQQ PWKGKIAGTR KTTPGFRLVE KLALLTAGLD THRMDLSSMI
MLKDNHIWAC GNITNTVKNA RSVGGFSLKI EVECRNQNEA IEAIEAGADI VMLDNFNPQD
LQTVSTYLKQ HYPHITLEAS GGITSATIIQ YAIPTIDIIS MGNLTQGVPH IDISLKIQKQ
