ID W6F9V1_BIFBR Unreviewed; 297 AA.
AC W6F9V1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=nicotinate-nucleotide diphosphorylase (carboxylating) {ECO:0000256|ARBA:ARBA00011944};
DE EC=2.4.2.19 {ECO:0000256|ARBA:ARBA00011944};
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000256|ARBA:ARBA00033102};
GN ORFNames=B7019_1401 {ECO:0000313|EMBL:AHJ19587.1};
OS Bifidobacterium breve JCM 7019.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1385940 {ECO:0000313|EMBL:AHJ19587.1, ECO:0000313|Proteomes:UP000019336};
RN [1] {ECO:0000313|EMBL:AHJ19587.1, ECO:0000313|Proteomes:UP000019336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7019 {ECO:0000313|EMBL:AHJ19587.1,
RC ECO:0000313|Proteomes:UP000019336};
RA Bottacini F.;
RT "The Bifidobacterium breve pan-genome.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC {ECO:0000256|ARBA:ARBA00003237}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004893}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family.
CC {ECO:0000256|ARBA:ARBA00009400, ECO:0000256|PIRNR:PIRNR006250}.
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DR EMBL; CP006713; AHJ19587.1; -; Genomic_DNA.
DR RefSeq; WP_003830608.1; NZ_CP006713.1.
DR AlphaFoldDB; W6F9V1; -.
DR KEGG; bbrc:B7019_1401; -.
DR PATRIC; fig|1385940.3.peg.1341; -.
DR HOGENOM; CLU_039622_0_1_11; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000019336; Chromosome.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT DOMAIN 20..108
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 133..295
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 147..149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 259..261
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 280..282
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ SEQUENCE 297 AA; 31737 MW; 46A4A7C71068B47C CRC64;
MLTQHIIHTA VEAALAEDAP YGDITCETTI PAGETGSAHL TARENGVMSG IEVFRAAFTT
QNPAVTVTAA IKDGERFQAG QVLATVTGPV RDLLTAERIA LNFTQRMSGI ATMTAAFVDA
VNAIYSDNYD GSVTRPHRYE RTRIVDTRKT TPGLRPFEKY AVVCGGGHNH RYGLSDAVMM
KDNHLAALAA HGIDLTGAIR HVREQVGHTT HIEVEVDSLE QIPAVLEGGA DTIMLDNFSL
DDTRRGVELI DGKAIVEASG NMNLERVPAV AAAGVDVISV GALTHSVRSI DLGLDWI
//
