NADA_LISIN
ID NADA_LISIN Reviewed; 366 AA.
AC Q929Z0;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
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}; OrderedLocusNames=lin2133;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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}.
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DR EMBL; AL596171; CAC97363.1; -; Genomic_DNA.
DR PIR; AC1699; AC1699.
DR RefSeq; WP_010991772.1; NC_003212.1.
DR AlphaFoldDB; Q929Z0; -.
DR SMR; Q929Z0; -.
DR STRING; 272626.lin2133; -.
DR EnsemblBacteria; CAC97363; CAC97363; CAC97363.
DR KEGG; lin:nadA; -.
DR eggNOG; COG0379; Bacteria.
DR HOGENOM; CLU_047382_2_0_9; -.
DR OMA; CFCSTMN; -.
DR OrthoDB; 613347at2; -.
DR UniPathway; UPA00253; UER00327.
DR Proteomes; UP000002513; 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..366
FT /note="Quinolinate synthase"
FT /id="PRO_0000155820"
FT BINDING 44
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 61
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 108
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 139..141
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 160
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 228
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 254..256
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 271
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT BINDING 318
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
SQ SEQUENCE 366 AA; 41229 MW; 5BC8223820AD85F8 CRC64;
MNLLEKVEQD TMPARYKHMT SQEMIARVTE IKAQLGEDLF IPCHHYQKDE VVPFADAIGD
SLQLAQIAAN NKKAKHIVFC GVHFMAETAD MLTTNEQIVT LPDMRAGCSM ADMADIHQLT
NAWPKLQHLF GDTILPVTYI NSTAAIKSFV GEHGGTTVTS SNATKIVSWA LQQKERIFFL
PDQHLGRNTA FELGIPLEHM AIWNPIKNEL EYDGNLDDCK VILWKGYCSV HQHFTVKNIE
NIRKNHPNMR IIVHPECTHE VVSLADDSGS TKKIVTEISN AAPGTEWAVG TEANLVGRII
QENPDKKIVS LNPFMCPCMT MNRIDLPHLL WTLEAIQNGE QRNQIKVDEH TTKFALKALE
RMLQLS
