NADA_GEOTN
ID NADA_GEOTN Reviewed; 367 AA.
AC A4IRC0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Quinolinate synthase {ECO:0000255|HAMAP-Rule:MF_00569};
DE EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00569};
GN Name=nadA {ECO:0000255|HAMAP-Rule:MF_00569}; OrderedLocusNames=GTNG_2529;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP-
CC Rule:MF_00569}.
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_00569};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25889;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00569};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00569};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00569};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00569}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00569}.
CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 3
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00569}.
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DR EMBL; CP000557; ABO67874.1; -; Genomic_DNA.
DR RefSeq; WP_011887898.1; NC_009328.1.
DR AlphaFoldDB; A4IRC0; -.
DR SMR; A4IRC0; -.
DR STRING; 420246.GTNG_2529; -.
DR EnsemblBacteria; ABO67874; ABO67874; GTNG_2529.
DR KEGG; gtn:GTNG_2529; -.
DR eggNOG; COG0379; Bacteria.
DR HOGENOM; CLU_047382_2_0_9; -.
DR OMA; CFCSTMN; -.
DR OrthoDB; 613347at2; -.
DR UniPathway; UPA00253; UER00327.
DR Proteomes; UP000001578; 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_00569; NadA_type3; 1.
DR InterPro; IPR003473; NadA.
DR InterPro; IPR036094; NadA_sf.
DR InterPro; IPR023515; Quinolinate_synth_A_type3.
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; Transferase.
FT CHAIN 1..367
FT /note="Quinolinate synthase"
FT /id="PRO_1000024992"
FT BINDING 45
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 62
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 140..142
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 161
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 229
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 255..257
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 272
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 319
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
SQ SEQUENCE 367 AA; 41446 MW; 267B6A4B846DDC25 CRC64;
MNVLEQFKQL DNMPEQYKTM DRDELEARAR AVKEQLGRRL FIPGHHYQKD EVIQFADATG
DSLQLAQLAA KNNEAEYIVF CGVHFMAETA DILTSEEQTV ILPDLRAGCS MADMADVFQV
ERAWAALTDR FGETILPLVY VNSTAAIKAF VGRNGGATVT SSNAQKMVAW AFSQKERIFF
LPDQHLGRNT AYALGVGLDE MAVWDPYEET LQGNGDFDKV KVILWKGHCS VHENFNVRQI
EHIRQTKPET KVIVHPECSW DVVQQADYAG STKYIIETIR NASPGSRWAI GTEMNLVNRL
MHEHPDKEII SLNPYMCPCL TMNRIDLPHF VWALESLSEG TVVNRITVPK EVAFEAKLAL
ERMLALA
