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Database: UniProt
Entry: A0A021VQQ7_9CELL
LinkDB: A0A021VQQ7_9CELL
Original site: A0A021VQQ7_9CELL 
ID   A0A021VQQ7_9CELL        Unreviewed;       303 AA.
AC   A0A021VQQ7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=N866_09295 {ECO:0000313|EMBL:EYR62355.1};
OS   Actinotalea ferrariae CF5-4.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Actinotalea.
OX   NCBI_TaxID=948458 {ECO:0000313|EMBL:EYR62355.1, ECO:0000313|Proteomes:UP000019753};
RN   [1] {ECO:0000313|EMBL:EYR62355.1, ECO:0000313|Proteomes:UP000019753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF5-4 {ECO:0000313|EMBL:EYR62355.1,
RC   ECO:0000313|Proteomes:UP000019753};
RA   Chen F., Li Y., Wang G.;
RT   "Actinotalea ferrariae CF5-4.";
RL   Submitted (JAN-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYR62355.1}.
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DR   EMBL; AXCW01000258; EYR62355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A021VQQ7; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000019753; 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   Reference proteome {ECO:0000313|Proteomes:UP000019753};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          33..126
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          128..297
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
SQ   SEQUENCE   303 AA;  31665 MW;  61EE91B06EF44B13 CRC64;
     MDTQPADPGP ALDPAWTTRA VRVALDEDLG PAPGRDVTTQ ATVDPGESGV AHLVARADGV
     LAGLPVVAEV LGQVAGRLGL PVPEVEVRVD DGARVARGDV LAVLRGPVQV LLVGERTLLN
     LTSRASGVAT HTRRWADALA GTGAQVLDTR KTTPGLRELE KYAVRCGGGT NKRMGLYDVA
     MVKDNHVVAA GSVAGAVEAV RRRFPDVAVQ VEADTLEQAV EALDVGADFL LLDNMPTALL
     REVVRVVRAR DGGDRVELEA TGNLTLDRAA EVAATGVDFL SVGALTHSSP ILDLALDLVE
     RQV
//
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