ID   NADA_VIBVU              Reviewed;         353 AA.
AC   Q8DAM0;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=VV1_2173;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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_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; AE016795; AAO10558.1; -; Genomic_DNA.
DR   RefSeq; WP_011080050.1; NC_004459.3.
DR   AlphaFoldDB; Q8DAM0; -.
DR   SMR; Q8DAM0; -.
DR   EnsemblBacteria; AAO10558; AAO10558; VV1_2173.
DR   KEGG; vvu:VV1_2173; -.
DR   HOGENOM; CLU_047382_1_0_6; -.
DR   OMA; CFCSTMN; -.
DR   UniPathway; UPA00253; UER00327.
DR   Proteomes; UP000002275; Chromosome 1.
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_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; Transferase.
FT   CHAIN           1..353
FT                   /note="Quinolinate synthase"
FT                   /id="PRO_0000155775"
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;  38544 MW;  985059ADA9B2F89A CRC64;
     MSHILDKIDT VYPFPPKPIP LTQDEKAAYI ASIKQLLNEK DAVLIAHYYT DPEIQALAEE
     TGGFVGDSLE MAKFGNRHPA GTLIIAGVRF MGESAKILTP EKRILMPTLE AECSLDLGCP
     ADKFTEFCDA HPDHTVVVYA NTSAAVKARA DWVVTSSIAL EIVEHLDAED KPIIWGPDRH
     LGSYIANKTG ADMLLWQGEC VVHDEFSADA LRKMKAVYPD AAILVHPESP ASVVELADAV
     GSTSQLIKAA KELPQQKMIV ATDKGIFFKM QQLVPEKELI EAPTAGAGAT CRSCAHCPWM
     AMNGLKAIET ALREGGEQHE IFVDEALRVK SLIPLNRMLD FAEKLNMQVK GNA