NADA_PYRFU
ID NADA_PYRFU Reviewed; 303 AA.
AC Q8TZL3;
DT 25-OCT-2002, 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:0000255|HAMAP-Rule:MF_00568, ECO:0000303|PubMed:23999292};
DE Short=QS {ECO:0000303|PubMed:23999292};
DE EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:23999292};
GN Name=nadA {ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000303|PubMed:23999292};
GN OrderedLocusNames=PF1977;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2] {ECO:0007744|PDB:4HHE}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, PATHWAY, AND SUBUNIT.
RX PubMed=23999292; DOI=10.1107/s090744491301247x;
RA Soriano E.V., Zhang Y., Colabroy K.L., Sanders J.M., Settembre E.C.,
RA Dorrestein P.C., Begley T.P., Ealick S.E.;
RT "Active-site models for complexes of quinolinate synthase with substrates
RT and intermediates.";
RL Acta Crystallogr. D 69:1685-1696(2013).
CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP-
CC Rule:MF_00568, ECO:0000269|PubMed:23999292}.
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_00568,
CC ECO:0000269|PubMed:23999292};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25889;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568,
CC ECO:0000269|PubMed:23999292};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568,
CC ECO:0000269|PubMed:23999292};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00568};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00568,
CC ECO:0000269|PubMed:23999292}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23999292}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00568}.
CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00568}.
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DR EMBL; AE009950; AAL82101.1; -; Genomic_DNA.
DR RefSeq; WP_011013119.1; NZ_CP023154.1.
DR PDB; 4HHE; X-ray; 2.80 A; A=1-303.
DR PDBsum; 4HHE; -.
DR AlphaFoldDB; Q8TZL3; -.
DR SMR; Q8TZL3; -.
DR STRING; 186497.PF1977; -.
DR PRIDE; Q8TZL3; -.
DR EnsemblBacteria; AAL82101; AAL82101; PF1977.
DR GeneID; 41713799; -.
DR KEGG; pfu:PF1977; -.
DR PATRIC; fig|186497.12.peg.2050; -.
DR eggNOG; arCOG04459; Archaea.
DR HOGENOM; CLU_047382_0_0_2; -.
DR OMA; CFCSTMN; -.
DR OrthoDB; 18897at2157; -.
DR PhylomeDB; Q8TZL3; -.
DR BRENDA; 2.5.1.72; 5243.
DR UniPathway; UPA00253; UER00327.
DR EvolutionaryTrace; Q8TZL3; -.
DR Proteomes; UP000001013; 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_00568; NadA_type2; 1.
DR InterPro; IPR003473; NadA.
DR InterPro; IPR036094; NadA_sf.
DR InterPro; IPR023066; Quinolinate_synth_type2.
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 3D-structure; 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..303
FT /note="Quinolinate synthase"
FT /id="PRO_0000155809"
FT BINDING 25
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 42
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 113..115
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 130
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 174
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 200..202
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 217
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 260
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT HELIX 2..18
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:4HHE"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 182..190
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:4HHE"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:4HHE"
FT HELIX 286..302
FT /evidence="ECO:0007829|PDB:4HHE"
SQ SEQUENCE 303 AA; 34405 MW; 488B122FD4F1271F CRC64;
MEKVEELKKE IERLKKERNA IILAHNYQLP EVQDVADFVG DSLELARKAT KVDADVIVFA
GVDFMAETAK ILNPDKIVLI PNKRATCAMA NMLKVKHILE AKKKYPNAPV VLYVNSTAET
KAYADVTVTS ANAVDIIRKL DSDVIIFGPD KNLAHYVAKV TGKTIIPIPP EGHCYVHKKF
TIEDVERAKK LHPNAKLMVH PECNPEVQEH ADIIVSTGGM IRRACEWDEW VVFTEREMVY
RLSKLYPNKK FYPAKEDAVC VGMKAITLQH VYESLRDMKY EVTVPEEIAE KARKAIERML
EMS
