NADA_VIBCH
ID NADA_VIBCH Reviewed; 353 AA.
AC Q9KR14;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Quinolinate synthase {ECO:0000255|HAMAP-Rule:MF_00567};
DE EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00567};
GN Name=nadA {ECO:0000255|HAMAP-Rule:MF_00567}; OrderedLocusNames=VC_1833;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP-
CC Rule:MF_00567}.
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_00567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25889;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00567};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00567};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00567};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00567}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00567}.
CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00567}.
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DR EMBL; AE003852; AAF94981.1; -; Genomic_DNA.
DR PIR; E82151; E82151.
DR RefSeq; NP_231467.1; NC_002505.1.
DR RefSeq; WP_000018291.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KR14; -.
DR SMR; Q9KR14; -.
DR STRING; 243277.VC_1833; -.
DR PRIDE; Q9KR14; -.
DR DNASU; 2613587; -.
DR EnsemblBacteria; AAF94981; AAF94981; VC_1833.
DR GeneID; 57740468; -.
DR KEGG; vch:VC_1833; -.
DR PATRIC; fig|243277.26.peg.1749; -.
DR eggNOG; COG0379; Bacteria.
DR HOGENOM; CLU_047382_1_0_6; -.
DR OMA; CFCSTMN; -.
DR BioCyc; VCHO:VC1833-MON; -.
DR UniPathway; UPA00253; UER00327.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008987; F:quinolinate synthetase A activity; IBA:GO_Central.
DR GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central.
DR Gene3D; 3.40.50.10800; -; 3.
DR HAMAP; MF_00567; NadA_type1; 1.
DR InterPro; IPR003473; NadA.
DR InterPro; IPR036094; NadA_sf.
DR InterPro; IPR023513; Quinolinate_synth_A_type1.
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..353
FT /note="Quinolinate synthase"
FT /id="PRO_0000155773"
FT BINDING 47
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT BINDING 68
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT BINDING 113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT BINDING 139..141
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT BINDING 156
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT BINDING 200
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT BINDING 226..228
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT BINDING 243
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT BINDING 297
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
SQ SEQUENCE 353 AA; 38609 MW; 81950C47672FAA86 CRC64;
MSHILDTINT VYPFPPKPIP LRDEEKQAYI AEIKQLLIEK DAVLIAHYYT DPEIQALAES
TGGFVGDSLE MAKFGNRYPA TTLIIAGVRF MGESAKILTP EKRILMPTLE AECSLDLGCP
ADKFTEFCDA HPDHTVVVYA NTSAAVKARA DWVVTSSIAL EIVEHLDSEG KPIIWGPDRH
LGAYIAKKTG ADMLLWQGEC VVHDEFSADA LRKMKALYPD AAILVHPESP ASVVELADAV
GSTSQLIKAA KTLPQQKMIV ATDKGIFFKM QQMVPEKELI EAPTAGAGAT CRSCAHCPWM
AMNGLQAIAQ ALREGGKQHE IFVDEALRVK SLIPLNRMLD FAEQLNLKVK GNA
