NADC_PIG
ID NADC_PIG Reviewed; 299 AA.
AC I3LK75; M1KCW7;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating] {ECO:0000305};
DE EC=2.4.2.19 {ECO:0000305|PubMed:23626766};
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000303|PubMed:23626766};
DE Short=QAPRTase {ECO:0000303|PubMed:23626766};
DE Short=QPRTase {ECO:0000305};
GN Name=QPRT {ECO:0000312|EMBL:AGF33488.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000312|Proteomes:UP000008227};
RN [1] {ECO:0000312|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000312|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AGF33488.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-288, X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS)
RP OF 5-288 IN COMPLEX WITH NICOTINATE MONONUCLEOTIDE, AND SUBUNIT.
RC TISSUE=Liver {ECO:0000312|EMBL:AGF33488.1};
RX PubMed=23626766; DOI=10.1371/journal.pone.0062027;
RA Youn H.S., Kim M.K., Kang G.B., Kim T.G., Lee J.G., An J.Y., Park K.R.,
RA Lee Y., Kang J.Y., Song H.E., Park I., Cho C., Fukuoka S., Eom S.H.;
RT "Crystal structure of Sus scrofa quinolinate phosphoribosyltransferase in
RT complex with nicotinate mononucleotide.";
RL PLoS ONE 8:E62027-E62027(2013).
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. {ECO:0000269|PubMed:23626766}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR EMBL; AEMK02000016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KC185402; AGF33488.1; -; mRNA.
DR RefSeq; XP_003354604.1; XM_003354556.3.
DR PDB; 4I9A; X-ray; 2.10 A; A/B=1-288.
DR PDBsum; 4I9A; -.
DR AlphaFoldDB; I3LK75; -.
DR SMR; I3LK75; -.
DR STRING; 9823.ENSSSCP00000024489; -.
DR PaxDb; I3LK75; -.
DR PeptideAtlas; I3LK75; -.
DR Ensembl; ENSSSCT00000028901; ENSSSCP00000024489; ENSSSCG00000027454.
DR Ensembl; ENSSSCT00035083639; ENSSSCP00035034776; ENSSSCG00035062217.
DR Ensembl; ENSSSCT00045036063; ENSSSCP00045025077; ENSSSCG00045021123.
DR Ensembl; ENSSSCT00065029104; ENSSSCP00065011890; ENSSSCG00065021888.
DR GeneID; 100623339; -.
DR KEGG; ssc:100623339; -.
DR CTD; 23475; -.
DR VGNC; VGNC:104041; QPRT.
DR eggNOG; KOG3008; Eukaryota.
DR GeneTree; ENSGT00390000002761; -.
DR HOGENOM; CLU_039622_1_1_1; -.
DR InParanoid; I3LK75; -.
DR OMA; DMIMLKD; -.
DR OrthoDB; 1263431at2759; -.
DR TreeFam; TF300845; -.
DR BRENDA; 2.4.2.19; 6170.
DR Reactome; R-SSC-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000008227; Chromosome 3.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000027454; Expressed in metanephros cortex and 22 other tissues.
DR ExpressionAtlas; I3LK75; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Nucleotide-binding;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..299
FT /note="Nicotinate-nucleotide pyrophosphorylase
FT [carboxylating]"
FT /id="PRO_0000449543"
FT REGION 8..12
FT /note="Important for hexamer formation"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 102
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000250|UniProtKB:Q15274"
FT BINDING 138..139
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000305|PubMed:23626766,
FT ECO:0007744|PDB:4I9A"
FT BINDING 160..161
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000305|PubMed:23626766,
FT ECO:0007744|PDB:4I9A"
FT BINDING 171
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000305|PubMed:23626766,
FT ECO:0007744|PDB:4I9A"
FT BINDING 201
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000305|PubMed:23626766,
FT ECO:0007744|PDB:4I9A"
FT BINDING 222
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000305|PubMed:23626766,
FT ECO:0007744|PDB:4I9A"
FT BINDING 248..250
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000305|PubMed:23626766,
FT ECO:0007744|PDB:4I9A"
FT BINDING 270
FT /ligand="quinolinate"
FT /ligand_id="ChEBI:CHEBI:29959"
FT /evidence="ECO:0000305|PubMed:23626766,
FT ECO:0007744|PDB:4I9A"
FT CONFLICT 53
FT /note="V -> I (in Ref. 2; AGF33488)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="Q -> R (in Ref. 2; AGF33488)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="E -> K (in Ref. 2; AGF33488)"
FT /evidence="ECO:0000305"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:4I9A"
FT HELIX 12..26
FT /evidence="ECO:0007829|PDB:4I9A"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:4I9A"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:4I9A"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:4I9A"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:4I9A"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:4I9A"
FT HELIX 94..127
FT /evidence="ECO:0007829|PDB:4I9A"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4I9A"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:4I9A"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4I9A"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:4I9A"
FT HELIX 181..192
FT /evidence="ECO:0007829|PDB:4I9A"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:4I9A"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:4I9A"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:4I9A"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:4I9A"
FT HELIX 226..239
FT /evidence="ECO:0007829|PDB:4I9A"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:4I9A"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4I9A"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:4I9A"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:4I9A"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:4I9A"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:4I9A"
SQ SEQUENCE 299 AA; 30994 MW; 3EB249F870BA1C0B CRC64;
MDPEGLALLL PPATLATLAD SWLREDCPGL NPVALVTGAA PSQAVLWAKS PGVLAGRPFF
DAIFAQVNCQ VSWFLPEGSK LVPVAKVAEV QGPAHCLLLG ERVALNMLAR CSGVASAAAT
AVETARGTGW AGHVAGTRKT TPGFRLVEKY GLLVGGATSH RYDLGGLVMV KDNHVVAAGG
VEQAVQGARR AANFALKVEV ECSSLQEALE AAEAGADLVL LDNFRPEELH PTAAALKAQF
PTVGVEASGG VTLDNLPQFC GPHIDVISLG MLTQAAPALD FSLKLFAEGT TPVPYARKS
