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Database: UniProt
Entry: A0A1S3IJY9_LINUN
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ID   A0A1S3IJY9_LINUN        Unreviewed;       303 AA.
AC   A0A1S3IJY9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating] {ECO:0000256|ARBA:ARBA00020990, ECO:0000256|PIRNR:PIRNR006250};
DE            EC=2.4.2.19 {ECO:0000256|ARBA:ARBA00011944, ECO:0000256|PIRNR:PIRNR006250};
DE   AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000256|ARBA:ARBA00033102, ECO:0000256|PIRNR:PIRNR006250};
GN   Name=LOC106165033 {ECO:0000313|RefSeq:XP_013398558.1,
GN   ECO:0000313|RefSeq:XP_013398560.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|RefSeq:XP_013398560.1};
RN   [1] {ECO:0000313|RefSeq:XP_013398558.1, ECO:0000313|RefSeq:XP_013398560.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013398558.1,
RC   ECO:0000313|RefSeq:XP_013398560.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC       {ECO:0000256|ARBA:ARBA00003237, 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|ARBA:ARBA00000260,
CC         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|ARBA:ARBA00011218, 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   RefSeq; XP_013398558.1; XM_013543104.2.
DR   RefSeq; XP_013398560.1; XM_013543106.2.
DR   STRING; 7574.A0A1S3IJY9; -.
DR   EnsemblMetazoa; g10762.t1; g10762.t1; g10762.
DR   EnsemblMetazoa; XM_013543104.2; XP_013398558.1; LOC106165033.
DR   EnsemblMetazoa; XM_013543106.2; XP_013398560.1; LOC106165033.
DR   GeneID; 106165033; -.
DR   KEGG; lak:106165033; -.
DR   OMA; DIVMCDN; -.
DR   OrthoDB; 5473389at2759; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000085678; Unplaced.
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   Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          40..116
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          118..288
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
SQ   SEQUENCE   303 AA;  33426 MW;  0EBD761536457491 CRC64;
     MALMTGSRSH IHMLHPVTLR EKVREWLKED TPNFDYGGFV VGEKIETAVL LCKSPGVLAG
     APFFEAVFNE LDCNVEWLVS DGVFMKPIFQ CAKVTGKVRH ILLGERVALN CITRSSGIAT
     LARRLKECAK QNNWHGEIAG TRKTTPGFRM VEKYALLVGG ISTHRYDLSS MIMLKDNHIW
     SSGNITQAVK DARSVGGFST KIEVECRSLE EALEAAAAGS EVVMLDNFHP EVLHNTASKV
     KEKYPHALIE ASGGVTEDSL PQYFGPCIDV ISLSKTTQGY QTVDFSLKIQ KSGHNPHNPL
     VEK
//
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