NADA_BACMK
ID NADA_BACMK Reviewed; 368 AA.
AC A9VIQ3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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};
GN OrderedLocusNames=BcerKBAB4_4274;
OS Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBAB4;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000903; ABY45433.1; -; Genomic_DNA.
DR RefSeq; WP_002192476.1; NC_010184.1.
DR AlphaFoldDB; A9VIQ3; -.
DR SMR; A9VIQ3; -.
DR STRING; 315730.BcerKBAB4_4274; -.
DR EnsemblBacteria; ABY45433; ABY45433; BcerKBAB4_4274.
DR KEGG; bwe:BcerKBAB4_4274; -.
DR eggNOG; COG0379; Bacteria.
DR HOGENOM; CLU_047382_2_0_9; -.
DR OMA; CFCSTMN; -.
DR UniPathway; UPA00253; UER00327.
DR Proteomes; UP000002154; 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..368
FT /note="Quinolinate synthase"
FT /id="PRO_1000129455"
FT BINDING 46
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 63
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 141..143
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 162
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 230
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 256..258
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 273
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 320
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
SQ SEQUENCE 368 AA; 41610 MW; E38678466BF2F628 CRC64;
MGILEKVQPI EVMLPERYQT MSILEMEERV REIKEKMGAL LFIPGHHYQK DEVVQFSDAA
GDSLQLAQVA ANNKEAKYIV FCGVHFMAET ADMLTTDDQI VILPDMRAGC SMADMADIEQ
TERAWKELAK LFGDTMIPLT YVNSTAAIKA FCGRNGGATV TSSNAKQMVS WAFTQKERLV
FLPDQHLGRN TAYDLGIPLE KMAVWNPHTD SLEYDGDIEE IQVILWKGHC SVHQNFTVKN
IENVRKNHPD MNIIVHPECC YEVVAASDYA GSTKYIIDMI EAAPAGSKWA IGTEMNLVNR
IIQQHPDKEI ISLNPFMCPC LTMNRIDLPH LLWALENIER GEQINVIRVE KQVTEEAVLA
LNRMLERV
