NADA_FUSNN
ID NADA_FUSNN Reviewed; 298 AA.
AC Q8R6C9;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Quinolinate synthase {ECO:0000250|UniProtKB:O57767};
DE EC=2.5.1.72 {ECO:0000250|UniProtKB:O57767};
GN Name=nadA; OrderedLocusNames=FN0008;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC dihydroxyacetone phosphate to form quinolinate.
CC {ECO:0000250|UniProtKB:O57767}.
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:0000250|UniProtKB:O57767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25889;
CC Evidence={ECO:0000250|UniProtKB:O57767};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:O57767};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:O57767};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC iminoaspartate: step 1/1. {ECO:0000250|UniProtKB:O57767}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; AE009951; AAL94221.1; -; Genomic_DNA.
DR RefSeq; NP_602922.1; NC_003454.1.
DR AlphaFoldDB; Q8R6C9; -.
DR SMR; Q8R6C9; -.
DR STRING; 190304.FN0008; -.
DR EnsemblBacteria; AAL94221; AAL94221; FN0008.
DR KEGG; fnu:FN0008; -.
DR PATRIC; fig|190304.8.peg.600; -.
DR eggNOG; COG0379; Bacteria.
DR HOGENOM; CLU_047382_0_0_0; -.
DR InParanoid; Q8R6C9; -.
DR OMA; CFCSTMN; -.
DR BioCyc; FNUC190304:G1FZS-622-MON; -.
DR UniPathway; UPA00253; UER00327.
DR Proteomes; UP000002521; 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 InterPro; IPR003473; NadA.
DR InterPro; IPR036094; NadA_sf.
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; Reference proteome; Transferase.
FT CHAIN 1..298
FT /note="Quinolinate synthase"
FT /id="PRO_0000155787"
FT BINDING 19
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 36
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 107..109
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 124
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 167
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 193..195
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 210
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000250|UniProtKB:O57767"
FT BINDING 253
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O57767"
SQ SEQUENCE 298 AA; 33814 MW; E92353C22ADE3801 CRC64;
MKDRIKKLQK EKDVAILAHY YVDGEVQEIA DYVGDSFYLA KTATKLKNKT IIMAGVYFMG
ESIKILNPEK MVHMVDIYAD CPMAHMITIK KIKEMREKYD DLAVVCYINS TAEIKAYCDV
CITSSNAVKI VSKLKEKNIF IVPDGNLASY ITKQVKNKNI ILNKGYCCVH NLVHLENVIK
LKNEYPNARV LAHPECKEEI LNLADYIGST SGIIEEVLKD GNEFIIVTER GIQHKIYEKA
PNKKLYFADT LICKSMKKNT LEKIEKILLD GGDELEVNDE IAKKALIPLE KMLELAGD
