NADA_BACSU
ID NADA_BACSU Reviewed; 368 AA.
AC Q9KWZ1; O32063;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Quinolinate synthase {ECO:0000255|HAMAP-Rule:MF_00569, ECO:0000303|PubMed:18959769};
DE EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00569, ECO:0000269|PubMed:18959769};
GN Name=nadA {ECO:0000255|HAMAP-Rule:MF_00569, ECO:0000303|PubMed:18959769};
GN OrderedLocusNames=BSU27850;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Tosato V., Bolotin A., Bertani I., Valentino I., Bruschi C.V.;
RT "A 17.8 kb segment in the spoVB-nadC region of the Bacillus subtilis 168
RT chromosome: sequencing and ruv operon identification.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, SUBUNIT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-82; CYS-110;
RP CYS-230; CYS-259; CYS-318 AND CYS-320.
RX PubMed=18959769; DOI=10.1111/j.1742-4658.2008.06641.x;
RA Marinoni I., Nonnis S., Monteferrante C., Heathcote P., Haertig E.,
RA Boettger L.H., Trautwein A.X., Negri A., Albertini A.M., Tedeschi G.;
RT "Characterization of L-aspartate oxidase and quinolinate synthase from
RT Bacillus subtilis.";
RL FEBS J. 275:5090-5107(2008).
CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP-
CC Rule:MF_00569, ECO:0000269|PubMed:18959769}.
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 ECO:0000269|PubMed:18959769};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25889;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00569,
CC ECO:0000269|PubMed:18959769};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00569,
CC ECO:0000269|PubMed:18959769};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00569, ECO:0000269|PubMed:18959769};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.36 mM for dihydroxyacetone phosphate
CC {ECO:0000269|PubMed:18959769};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00569,
CC ECO:0000269|PubMed:18959769}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:18959769}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00569}.
CC -!- DISRUPTION PHENOTYPE: Mutant requires exogenous nicotinic acid for
CC growth. {ECO:0000269|PubMed:18959769}.
CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 3
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00569}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB75321.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y15896; CAB75321.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB14745.1; -; Genomic_DNA.
DR PIR; E69663; E69663.
DR RefSeq; NP_390663.1; NC_000964.3.
DR RefSeq; WP_003229691.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; Q9KWZ1; -.
DR SMR; Q9KWZ1; -.
DR IntAct; Q9KWZ1; 1.
DR MINT; Q9KWZ1; -.
DR STRING; 224308.BSU27850; -.
DR PaxDb; Q9KWZ1; -.
DR PRIDE; Q9KWZ1; -.
DR DNASU; 937522; -.
DR EnsemblBacteria; CAB14745; CAB14745; BSU_27850.
DR GeneID; 937522; -.
DR KEGG; bsu:BSU27850; -.
DR PATRIC; fig|224308.179.peg.3026; -.
DR eggNOG; COG0379; Bacteria.
DR InParanoid; Q9KWZ1; -.
DR OMA; CFCSTMN; -.
DR PhylomeDB; Q9KWZ1; -.
DR BioCyc; BSUB:BSU27850-MON; -.
DR UniPathway; UPA00253; UER00327.
DR Proteomes; UP000001570; 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_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 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..368
FT /note="Quinolinate synthase"
FT /id="PRO_0000155816"
FT BINDING 46
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767, ECO:0000255|HAMAP-
FT Rule:MF_00569"
FT BINDING 63
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767, ECO:0000255|HAMAP-
FT Rule:MF_00569"
FT BINDING 110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569,
FT ECO:0000269|PubMed:18959769"
FT BINDING 141..143
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767, ECO:0000255|HAMAP-
FT Rule:MF_00569"
FT BINDING 162
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767, ECO:0000255|HAMAP-
FT Rule:MF_00569"
FT BINDING 230
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569,
FT ECO:0000269|PubMed:18959769"
FT BINDING 256..258
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767, ECO:0000255|HAMAP-
FT Rule:MF_00569"
FT BINDING 273
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767, ECO:0000255|HAMAP-
FT Rule:MF_00569"
FT BINDING 320
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569,
FT ECO:0000269|PubMed:18959769"
FT MUTAGEN 82
FT /note="C->S: No change in activity and in iron content."
FT /evidence="ECO:0000269|PubMed:18959769"
FT MUTAGEN 110
FT /note="C->S: Loss of activity. Does not bind iron. Cannot
FT complement the deletion mutant."
FT /evidence="ECO:0000269|PubMed:18959769"
FT MUTAGEN 230
FT /note="C->S: Loss of activity. Does not bind iron. Cannot
FT complement the deletion mutant."
FT /evidence="ECO:0000269|PubMed:18959769"
FT MUTAGEN 259
FT /note="C->S: No change in activity and in iron content."
FT /evidence="ECO:0000269|PubMed:18959769"
FT MUTAGEN 318
FT /note="C->S: No change in activity and in iron content.
FT Cannot complement the deletion mutant. Lacks activity and
FT does not binds iron; when associated with S-320."
FT /evidence="ECO:0000269|PubMed:18959769"
FT MUTAGEN 320
FT /note="C->S: Loss of activity. Decreases iron binding.
FT Cannot complement the deletion mutant. Lacks activity and
FT does not binds iron; when associated with S-318."
FT /evidence="ECO:0000269|PubMed:18959769"
SQ SEQUENCE 368 AA; 41493 MW; 7F2E428C69B8A567 CRC64;
MSILDVIKQS NDMMPESYKE LSRKDMETRV AAIKKKFGSR LFIPGHHYQK DEVIQFADQT
GDSLQLAQVA EKNKEADYIV FCGVHFMAET ADMLTSEQQT VVLPDMRAGC SMADMADMQQ
TNRAWKKLQH IFGDTIIPLT YVNSTAEIKA FVGKHGGATV TSSNAKKVLE WAFTQKKRIL
FLPDQHLGRN TAYDLGIALE DMAVWDPMKD ELVAESGHTN VKVILWKGHC SVHEKFTTKN
IHDMRERDPD IQIIVHPECS HEVVTLSDDN GSTKYIIDTI NQAPAGSKWA IGTEMNLVQR
IIHEHPDKQI ESLNPDMCPC LTMNRIDLPH LLWSLEQIEK GEPSGVIKVP KAIQEDALLA
LNRMLSIT
