ID E8PQR4_THESS Unreviewed; 286 AA.
AC E8PQR4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 66.
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:ADW21846.1};
GN OrderedLocusNames=TSC_c12260 {ECO:0000313|EMBL:ADW21846.1};
OS Thermus scotoductus (strain ATCC 700910 / SA-01).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=743525 {ECO:0000313|EMBL:ADW21846.1, ECO:0000313|Proteomes:UP000008087};
RN [1] {ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RA Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
RA Gottschalk G., van Heerden E., Litthauer D.;
RT "The genome sequence of Thermus scotoductus SA-01.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADW21846.1, ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RX PubMed=22115438; DOI=10.1186/1471-2164-12-577;
RA Gounder K., Brzuszkiewicz E., Liesegang H., Wollherr A., Daniel R.,
RA Gottschalk G., Reva O., Kumwenda B., Srivastava M., Bricio C.,
RA Berenguer J., van Heerden E., Litthauer D.;
RT "Sequence of the hyperplastic genome of the naturally competent Thermus
RT scotoductus SA-01.";
RL BMC Genomics 12:577-577(2011).
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; CP001962; ADW21846.1; -; Genomic_DNA.
DR RefSeq; WP_015717123.1; NC_014974.1.
DR AlphaFoldDB; E8PQR4; -.
DR STRING; 743525.TSC_c12260; -.
DR KEGG; tsc:TSC_c12260; -.
DR eggNOG; COG0157; Bacteria.
DR HOGENOM; CLU_039622_0_1_0; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000008087; 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 27..115
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 117..281
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 138..140
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 246..248
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT BINDING 267..269
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ SEQUENCE 286 AA; 30709 MW; 19167ADEC6DE0331 CRC64;
MEPPASPRIG PMVPLETLKA WLLEDLGHGD LTTALTVPED LMGEAVILAK EEGVLAGLPV
AREVFTLVDH RIAFTPLVEE GTKVDPGHEV ARLEGPLRGI LAGERLALNL LQRLSGIATL
TRAYVEALKG TKAQVLDTRK TTPGLRALEK YAVRVGEGKN HRFGLFDGIL IKENHIRAAG
GVAQAVRKAK AKAPHYLKVE VEVTRLAELE EALEAGADLI LLDNFSLEEM REAVRRVGGR
VPLEASGNMT LERARAAAEA GVDYVSVGAL THSAKALDLS LLVVQP
//
