ID   NADA_SHESM              Reviewed;         357 AA.
AC   Q0HIL9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
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};
GN   OrderedLocusNames=Shewmr4_2025;
OS   Shewanella sp. (strain MR-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. MR-4.";
RL   Submitted (AUG-2006) 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; CP000446; ABI39098.1; -; Genomic_DNA.
DR   RefSeq; WP_011622789.1; NC_008321.1.
DR   AlphaFoldDB; Q0HIL9; -.
DR   SMR; Q0HIL9; -.
DR   KEGG; she:Shewmr4_2025; -.
DR   HOGENOM; CLU_047382_1_0_6; -.
DR   OMA; CFCSTMN; -.
DR   UniPathway; UPA00253; UER00327.
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..357
FT                   /note="Quinolinate synthase"
FT                   /id="PRO_1000024971"
FT   BINDING         50
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT   BINDING         71
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT   BINDING         116
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT   BINDING         142..144
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT   BINDING         159
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT   BINDING         203
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT   BINDING         229..231
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT   BINDING         246
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
FT   BINDING         300
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00567"
SQ   SEQUENCE   357 AA;  38762 MW;  A42016AF49E7656E CRC64;
     MSPSPFAPTI ETIDYPFPPK PIPLSDAEKA DYKARIKQLL IEKDAVLVAH YYTDPEIQAL
     AEETGGCVSD SLEMARFGRD HPAKTLIVAG VKFMGETAKI LSPEKTILMP TLEATCSLDL
     GCPIDKFSAF CDAHPDHTVV VYANTSAAVK ARADWVVTSS IALEIVEHLD SEGKKIIWGP
     DRHLGSYIAK QTGAEMLMWQ GDCIVHDEFK ANALRDLKRV YPDAAILVHP ESPASVVAMA
     DAVGSTSQLI KAAQTMANER FIVATDRGIF YKMQQAAPGK TLIEAPTGGN GATCKSCAHC
     PWMAMNGLKA IEASLSDSDK TTHEIFVDED LRVKALIPLT RMLDFAKTLN MKVKGNA