NADC_NEMVE
ID NADC_NEMVE Reviewed; 289 AA.
AC A7SG73;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating];
DE EC=2.4.2.19;
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating];
DE Short=QAPRTase;
DE Flags: Fragment;
GN Name=qprt; ORFNames=v1g117116;
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6;
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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; DS469650; EDO37262.1; -; Genomic_DNA.
DR RefSeq; XP_001629325.1; XM_001629275.1.
DR AlphaFoldDB; A7SG73; -.
DR SMR; A7SG73; -.
DR STRING; 45351.EDO37262; -.
DR EnsemblMetazoa; EDO37262; EDO37262; NEMVEDRAFT_v1g117116.
DR GeneID; 5508760; -.
DR KEGG; nve:5508760; -.
DR eggNOG; KOG3008; Eukaryota.
DR HOGENOM; CLU_039622_1_0_1; -.
DR InParanoid; A7SG73; -.
DR OMA; DMIMLKD; -.
DR OrthoDB; 1263431at2759; -.
DR PhylomeDB; A7SG73; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IBA:GO_Central.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
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..>289
FT /note="Nicotinate-nucleotide pyrophosphorylase
FT [carboxylating]"
FT /id="PRO_0000327817"
FT REGION 12..16
FT /note="Important for hexamer formation"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 106
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 142..143
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 164..165
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 175
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 205
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 226
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 252..254
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 274
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT NON_TER 289
SQ SEQUENCE 289 AA; 31464 MW; 70CA3E9919949B3C CRC64;
MADESAFRNF SLLIPKVVIE KHVETWLKED TPSFDYGGFV VGSSVEKAVL LCKSDGVLAG
VPFFNAIFEK LDCKVEWQNN EGDPIKAVSV IGTVTGPVNK ILLGERVALN CISRASGIAT
KSRSLTNLKE QYQWHGEIAG TRKTTPGFRV VEKYALEVGG VSTHRYDLST MIMLKDNHIW
STGNITRAVK NARRVGGFSM KIEVECRSLE EALEAAHAGA EIVMLDNFEP QALHTTAKTL
KGKCAGVIIE ASGGINDSSI AQYFGPHVDV ISLGCLTQGY KPVNFSLKI
