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Database: UniProt
Entry: A0A179V0I2_BLAGS
LinkDB: A0A179V0I2_BLAGS
Original site: A0A179V0I2_BLAGS 
ID   A0A179V0I2_BLAGS        Unreviewed;       311 AA.
AC   A0A179V0I2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=BDBG_08974 {ECO:0000313|EMBL:OAT13854.1};
OS   Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT13854.1, ECO:0000313|Proteomes:UP000002038};
RN   [1] {ECO:0000313|Proteomes:UP000002038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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; GG657479; OAT13854.1; -; Genomic_DNA.
DR   RefSeq; XP_002620679.1; XM_002620633.1.
DR   AlphaFoldDB; A0A179V0I2; -.
DR   STRING; 559298.A0A179V0I2; -.
DR   GeneID; 8501291; -.
DR   KEGG; bgh:BDBG_08974; -.
DR   VEuPathDB; FungiDB:BDBG_08974; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000002038; Unassembled WGS sequence.
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:UP000002038};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          36..113
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          115..307
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
SQ   SEQUENCE   311 AA;  33018 MW;  5FAC1B5D15F3A386 CRC64;
     MASLHGDLSH LLPLNFKHTI TAWLEEDCPS FDYGGFVVGE AEGEAKLLGK SKGVVAGVPF
     FNEVFSQLGC TVEWKVKEGE PIEPITVCAI VRGPMRKILL GERVALNILA RCSGIATKTS
     TLVNILRSHS WNGILAGTRK TTPGFRLVEK YGILVGGADP HRHDLSSMTM LKDNHIWACY
     NKGQVQSATA ASIAQAIPTA VEAARAAAGF STKVEVECRS IEEAHAAISA GANIIMLDNF
     SASEVAGAAK LLKDEWTAKG KPRGSFLVEV SGGLNEQNAA SFAAEDVDIL STSSIHQGVG
     IVDFSLKVSL T
//
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