(data stored in ACNUC7421 zone)

SWISSPROT: NADA_ECO27

ID   NADA_ECO27              Reviewed;         347 AA.
AC   B7ULM3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   05-DEC-2018, entry version 58.
DE   RecName: Full=Quinolinate synthase A {ECO:0000255|HAMAP-Rule:MF_00567};
DE            EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00567};
GN   Name=nadA {ECO:0000255|HAMAP-Rule:MF_00567};
GN   OrderedLocusNames=E2348C_0627;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC       dihydroxyacetone phosphate to form quinolinate.
CC       {ECO:0000255|HAMAP-Rule:MF_00567}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dihydroxyacetone phosphate + iminosuccinate = H(+) + 2
CC         H2O + phosphate + quinolinate; Xref=Rhea:RHEA:25888,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29959,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57642, ChEBI:CHEBI:77875;
CC         EC=2.5.1.72; Evidence={ECO:0000255|HAMAP-Rule:MF_00567};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00567};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00567};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00567}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00567}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00567}.
CC   -!- SIMILARITY: Belongs to the quinolinate synthase A family. Type 1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00567}.
DR   EMBL; FM180568; CAS08175.1; -; Genomic_DNA.
DR   RefSeq; WP_000115299.1; NC_011601.1.
DR   SMR; B7ULM3; -.
DR   PRIDE; B7ULM3; -.
DR   EnsemblBacteria; CAS08175; CAS08175; E2348C_0627.
DR   KEGG; ecg:E2348C_0627; -.
DR   KO; K03517; -.
DR   OMA; LWAPDRH; -.
DR   BioCyc; ECOL574521:E2348C_RS03365-MONOMER; -.
DR   UniPathway; UPA00253; UER00327.
DR   Proteomes; UP000008205; 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   HAMAP; MF_00567; NadA_type1; 1.
DR   InterPro; IPR003473; NadA.
DR   InterPro; IPR036094; NadA_sf.
DR   InterPro; IPR023513; Quinolinate_synth_A_type1.
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;
DR   PRODOM; B7ULM3.
DR   SWISS-2DPAGE; B7ULM3.
KW   4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN         1    347       Quinolinate synthase A.
FT                                /FTId=PRO_1000146804.
FT   BINDING      47     47       Iminoaspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00567}.
FT   BINDING      68     68       Iminoaspartate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00567}.
FT   BINDING     139    139       Iminoaspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00567}.
FT   BINDING     156    156       Iminoaspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00567}.
FT   BINDING     226    226       Iminoaspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00567}.
FT   BINDING     243    243       Iminoaspartate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00567}.
SQ   SEQUENCE   347 AA;  38299 MW;  F0EEF18B64206C9E CRC64;
     MSVMFDPDTA IYPFPPKPTP LSIDEKAYYR EKIKRLLKER NAVMVAHYYT DPEIQQLAEE
     TGGCISDSLE MARFGAKHPA STLLVAGVRF MGETAKILSP EKTILMPTLQ AECSLDLGCP
     VEEFNAFCDA HPDRTVVVYA NTSAAVKARA DWVVTSSIAV ELIDHLDSLG EKIIWAPDTH
     LGRYVQKQTG ADILCWQGAC IVHDEFKTQA LTRLQEEYPD AAILVHPESP QAIVEMADAV
     GSTSQLIAAA KTLQHQRLIV ATDRGIFYKM QQAVPDKELL EAPTAGEGAT CRSCAHCPWM
     AMNGLQAIAE ALEQEGSNHE VYVDERLRER ALVPLNRMLD FAATLRG
//

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