ID A0A1M5C544_9FIRM Unreviewed; 285 AA.
AC A0A1M5C544;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN02745133_02802 {ECO:0000313|EMBL:SHF49756.1};
OS Desulforamulus putei DSM 12395.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1121429 {ECO:0000313|EMBL:SHF49756.1, ECO:0000313|Proteomes:UP000184148};
RN [1] {ECO:0000313|EMBL:SHF49756.1, ECO:0000313|Proteomes:UP000184148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12395 {ECO:0000313|EMBL:SHF49756.1,
RC ECO:0000313|Proteomes:UP000184148};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQUY01000028; SHF49756.1; -; Genomic_DNA.
DR RefSeq; WP_073239997.1; NZ_FQUY01000028.1.
DR AlphaFoldDB; A0A1M5C544; -.
DR STRING; 1121429.SAMN02745133_02802; -.
DR OrthoDB; 9782546at2; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000184148; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT DOMAIN 20..109
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 111..276
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 132..134
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 240..242
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 261..263
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ SEQUENCE 285 AA; 30243 MW; EEA22C929BD4A3C0 CRC64;
MELNMFELNK LIATSLAEDI GTGDITTNSI VPAGSVAKGI IYVKEPGIVA GIPVAEAVFR
YLAPDIGFSA RVQDGASLEP GDVIAEVEGD ARAILTGERL ALNFLQRMSG IATRTAALVD
KVKLYPVRVV DTRKTTPGLR MLEKYAVRVG GGFNHRFGLY DAVLIKDNHI KVAGGITQAV
LAARQNVPHT VKIEVEVENL AGVNEALEAR ADVIMLDNMD PATMREAVKL VDGRALVEAS
GGINEETITA VAKAGVDLIS IGALTHSIKS LDISLDIGEI KSHKP
//
