NADA_CYAPA
ID NADA_CYAPA Reviewed; 329 AA.
AC P31179;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Quinolinate synthase {ECO:0000255|HAMAP-Rule:MF_00568};
DE EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00568};
GN Name=nadA {ECO:0000255|HAMAP-Rule:MF_00568};
OS Cyanophora paradoxa.
OG Plastid; Cyanelle.
OC Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX NCBI_TaxID=2762;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UTEX LB 555 / Pringsheim;
RX PubMed=1711042; DOI=10.1016/s0021-9258(18)99037-x;
RA Michalowski C.B., Loeffelhardt W., Bohnert H.J.;
RT "An ORF323 with homology to crtE, specifying prephytoene pyrophosphate
RT dehydrogenase, is encoded by cyanelle DNA in the eukaryotic alga Cyanophora
RT paradoxa.";
RL J. Biol. Chem. 266:11866-11870(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX LB 555 / Pringsheim;
RA Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J.,
RA Bryant D.A.;
RT "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa.";
RL Plant Mol. Biol. Rep. 13:327-332(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX LB 555 / Pringsheim;
RA Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M.,
RA Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M.,
RA Jakowitsch J., Bohnert H.J., Bryant D.A.;
RT "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the
RT genetic complexity of a primitive plastid.";
RL (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W.
RL (eds.);
RL Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997).
CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP-
CC Rule:MF_00568}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25889;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568};
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 -!- SUBCELLULAR LOCATION: Plastid, cyanelle.
CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00568}.
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DR EMBL; M37111; AAA65473.1; -; Genomic_DNA.
DR EMBL; U30821; AAA81216.1; -; Genomic_DNA.
DR PIR; C40433; C40433.
DR PIR; T06873; T06873.
DR RefSeq; NP_043185.1; NC_001675.1.
DR AlphaFoldDB; P31179; -.
DR SMR; P31179; -.
DR GeneID; 801687; -.
DR BRENDA; 2.5.1.72; 1772.
DR UniPathway; UPA00253; UER00327.
DR GO; GO:0009842; C:cyanelle; 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 3: Inferred from homology;
KW 4Fe-4S; Cyanelle; Iron; Iron-sulfur; Metal-binding; Plastid;
KW Pyridine nucleotide biosynthesis; Transferase.
FT CHAIN 1..329
FT /note="Quinolinate synthase"
FT /id="PRO_0000155814"
FT BINDING 44
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 61
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 132..134
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 149
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 218..220
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 235
FT /ligand="iminosuccinate"
FT /ligand_id="ChEBI:CHEBI:77875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT BINDING 285
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
SQ SEQUENCE 329 AA; 36805 MW; BFF8124E292F8095 CRC64;
MSIFLKNKQF ENITSQEQTK NNYKQLINDI QTLKKDLNAI ILAHYYQEPD IQDVADFLGD
SLGLAREAAK TNADIIVFAG VHFMAETAKI LNPEKMVLLP DLNAGCSLAD SCPPEIFSEF
KKAHSDHLVI SYINCSASIK AMSDIICTSA NAVDIVNKIP LTQPILFAPD QNLGRYVISK
TGRDLLLWPG SCIVHETFSE KKIFEFQSLY PTAEVIAHPE CEPTILKHAN YIGSTTSLLQ
YVKNSKKTTF IVITEPGIIH QMKKSCPEKQ FLALPTVSGC ACNECPHMRL NTLEKLYLAM
KTRSPQIEIP ESILLNAKKP IERMLEMSN
