ID A0A2W1JDF2_9CYAN Unreviewed; 288 AA.
AC A0A2W1JDF2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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_1 {ECO:0000313|EMBL:PZD71788.1};
GN ORFNames=C1752_04430 {ECO:0000313|EMBL:PZD71788.1};
OS Acaryochloris thomasi RCC1774.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris; Acaryochloris thomasi.
OX NCBI_TaxID=1764569 {ECO:0000313|EMBL:PZD71788.1, ECO:0000313|Proteomes:UP000248857};
RN [1] {ECO:0000313|EMBL:PZD71788.1, ECO:0000313|Proteomes:UP000248857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC1774 {ECO:0000313|EMBL:PZD71788.1,
RC ECO:0000313|Proteomes:UP000248857};
RX PubMed=29904088; DOI=10.1038/s41598-018-27542-7;
RA Partensky F., Six C., Ratin M., Garczarek L., Vaulot D., Probert I.,
RA Calteau A., Gourvil P., Marie D., Grebert T., Bouchier C., Le Panse S.,
RA Gachenot M., Rodriguez F., Garrido J.L.;
RT "A novel species of the marine cyanobacterium Acaryochloris with a unique
RT pigment content and lifestyle.";
RL Sci. Rep. 8:9142-9142(2018).
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:PZD71788.1}.
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DR EMBL; PQWO01000014; PZD71788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1JDF2; -.
DR OrthoDB; 9782546at2; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000248857; 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:UP000248857};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT DOMAIN 27..115
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 117..285
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
SQ SEQUENCE 288 AA; 30912 MW; 5ECE7FD0F3738B94 CRC64;
MDSSVPATLP AWIILDPMLT RWLQEDIGRG DLTTQALGLS EQGQAKLLFK QAGCVAGLPL
VQRVFSLLDG HIKLMPLVAE GEWCAAGTVV AELQGPMAPL LTGERVALNL IMRLSGIATL
TKQYGDAIAT LPTQLVDTRK TTPGLRLLEK YATRIGGAKN HRLGLDDAVM LKDNHIQAAG
GIGAAIDQVR TQIPYPLAVE VETETLEQVT EALEHDVDII MLDNMLPAQM QKAVGMIRAC
STTIKIEASG NITLDTIRAA AETGVDYIST SAPITQAPWL DISLRMIA
//