NADA_SALTY
ID NADA_SALTY Reviewed; 347 AA.
AC P24519;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 133.
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=STM0756;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=2198247; DOI=10.1128/jb.172.8.4187-4196.1990;
RA Foster J.W., Park Y.K., Penfound T., Fenger T., Spector M.P.;
RT "Regulation of NAD metabolism in Salmonella typhimurium: molecular sequence
RT analysis of the bifunctional nadR regulator and the nadA-pnuC operon.";
RL J. Bacteriol. 172:4187-4196(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 -!- INDUCTION: Repressed by NadR and partially controlled by cAMP.
CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00567}.
CC -!- SEQUENCE CAUTION:
CC Sequence=M85180; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M85180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE006468; AAL19695.1; -; Genomic_DNA.
DR PIR; C37753; C37753.
DR RefSeq; NP_459736.1; NC_003197.2.
DR RefSeq; WP_000115347.1; NC_003197.2.
DR AlphaFoldDB; P24519; -.
DR SMR; P24519; -.
DR STRING; 99287.STM0756; -.
DR PaxDb; P24519; -.
DR DNASU; 1252276; -.
DR EnsemblBacteria; AAL19695; AAL19695; STM0756.
DR GeneID; 1252276; -.
DR KEGG; stm:STM0756; -.
DR PATRIC; fig|99287.12.peg.787; -.
DR HOGENOM; CLU_047382_1_0_6; -.
DR OMA; CFCSTMN; -.
DR PhylomeDB; P24519; -.
DR BioCyc; SENT99287:STM0756-MON; -.
DR UniPathway; UPA00253; UER00327.
DR Proteomes; UP000001014; Chromosome.
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 2: Evidence at transcript level;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..347
FT /note="Quinolinate synthase"
FT /id="PRO_0000155770"
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 347 AA; 37944 MW; 35D1D22898FCCC22 CRC64;
MSVMFDPQAA IYPFPPKPTP LNDDEKQFYR EKIKRLLKER NAVMVAHYYT DPEIQQLAEE
TGGCISDSLE MARFGTKHAA STLLVAGVRF MGETAKILSP EKTILMPTLA AECSLDLGCP
IDEFSAFCDA HPDRTVVVYA NTSAAVKARA DWVVTSSIAV ELIEHLDSLG EKIIWAPDRH
LGNYVQKQTG ADVLCWQGAC IVHDEFKTQA LTRLKKIYPD AALLVHPESP QSIVEMADAV
GSTSQLIKAA KTLPHRQLIV ATDRGIFYKM QQAVPEKELL EAPTAGEGAT CRSCAHCPWM
AMNGLKAIAE GLEQGGAAHE IQVDAALREG ALLPLNRMLD FAATLRA
