NADA_THET8
ID NADA_THET8 Reviewed; 310 AA.
AC Q5SJM4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Quinolinate synthase {ECO:0000255|HAMAP-Rule:MF_00568};
DE EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00568};
GN Name=nadA {ECO:0000255|HAMAP-Rule:MF_00568}; OrderedLocusNames=TTHA0984;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP-
CC Rule:MF_00568}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O +
CC phosphate + quinolinate; Xref=Rhea:RHEA:25888, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29959, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:77875; EC=2.5.1.72;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25889;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00568};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00568}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00568}.
CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00568}.
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DR EMBL; AP008226; BAD70807.1; -; Genomic_DNA.
DR RefSeq; WP_011228349.1; NC_006461.1.
DR RefSeq; YP_144250.1; NC_006461.1.
DR AlphaFoldDB; Q5SJM4; -.
DR SMR; Q5SJM4; -.
DR STRING; 300852.55772366; -.
DR EnsemblBacteria; BAD70807; BAD70807; BAD70807.
DR GeneID; 3168272; -.
DR KEGG; ttj:TTHA0984; -.
DR PATRIC; fig|300852.9.peg.966; -.
DR eggNOG; COG0379; Bacteria.
DR HOGENOM; CLU_047382_0_0_0; -.
DR OMA; CFCSTMN; -.
DR PhylomeDB; Q5SJM4; -.
DR UniPathway; UPA00253; UER00327.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008987; F:quinolinate synthetase A activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10800; -; 3.
DR HAMAP; MF_00568; NadA_type2; 1.
DR InterPro; IPR003473; NadA.
DR InterPro; IPR036094; NadA_sf.
DR InterPro; IPR023066; Quinolinate_synth_type2.
DR PANTHER; PTHR30573; PTHR30573; 1.
DR Pfam; PF02445; NadA; 1.
DR SUPFAM; SSF142754; SSF142754; 1.
DR TIGRFAMs; TIGR00550; nadA; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..310
FT /note="Quinolinate synthase"
FT /id="PRO_1000072575"
FT BINDING 27
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 44
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 115..117
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 132
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 201..203
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 222
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 267
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
SQ SEQUENCE 310 AA; 34181 MW; 4F95AF26002BDFD4 CRC64;
MGRMRGEALA QEVLRLKRER NAVILAHSYQ LPEVQEVADF VGDSLGLARE AQRTRAEVIV
FCGVHFMAET AAILNPEKTV LLPDLEAGCS LADSIRPEDV LAWKAKHPDG IVVAYVNTKA
EVKALADVCV TSANAVEVVS RLPQDRPIYF VPDMFLGAHV ARVTGRRLDL FPGECHVHAG
IREEHLKALL EAHPGAEFLI HPECGCGSGC LYLKPDAKML STEGMVRYAK GAEAREFVVA
TEVGILHRLK KEAPEKAFFP VKPDAVCEYM KRITLEKVYL SLKEMRHVVR VPEEVAGRAR
RALEAMVAVG
