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Database: UniProt
Entry: Q2KV47_BORA1
LinkDB: Q2KV47_BORA1
Original site: Q2KV47_BORA1 
ID   Q2KV47_BORA1            Unreviewed;       296 AA.
AC   Q2KV47;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
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   Name=nadC {ECO:0000313|EMBL:CAJ50551.1};
GN   OrderedLocusNames=BAV2941 {ECO:0000313|EMBL:CAJ50551.1};
OS   Bordetella avium (strain 197N).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ50551.1, ECO:0000313|Proteomes:UP000001977};
RN   [1] {ECO:0000313|EMBL:CAJ50551.1, ECO:0000313|Proteomes:UP000001977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N {ECO:0000313|EMBL:CAJ50551.1,
RC   ECO:0000313|Proteomes:UP000001977};
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ50551.1; -; Genomic_DNA.
DR   RefSeq; WP_012418580.1; NC_010645.1.
DR   AlphaFoldDB; Q2KV47; -.
DR   STRING; 360910.BAV2941; -.
DR   GeneID; 41394780; -.
DR   KEGG; bav:BAV2941; -.
DR   eggNOG; COG0157; Bacteria.
DR   HOGENOM; CLU_039622_0_1_4; -.
DR   OrthoDB; 9782546at2; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000001977; 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   Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          40..128
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          130..295
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
SQ   SEQUENCE   296 AA;  31156 MW;  C4868C91D0C81848 CRC64;
     MSIKTVSPTP ALETARVVPA LPQVMLEPLV RAALLEDLGR AGDITSDAIV PAEARGQTRL
     VARQAGVLAG LDLARLAFRL IDPEIRFQAR LTDGARLEPG SEIARIEGSA RGMLTAERTA
     LNFLGHLSGV ATGTASIADA IAHTACKVTC TRKTMPGLRA VQKYAVRVGG GSNHRYGLDD
     AVLIKDNHIA FAGGVTQALA RARASVGHMV KIELEVDTLD QLDEALASGV DVVLLDNMDH
     DTLREAVRRV DGRAITEASG RIAPETAAAI AETGVDLMAV GWLTHSARVL DIGLDS
//
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