(data stored in SCRATCH zone)

SWISSPROT: Q47SF4_THEFY

ID   Q47SF4_THEFY            Unreviewed;       332 AA.
AC   Q47SF4;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 103.
DE   RecName: Full=Quinolinate synthase A {ECO:0000256|HAMAP-Rule:MF_00568};
DE            EC=2.5.1.72 {ECO:0000256|HAMAP-Rule:MF_00568};
GN   Name=nadA {ECO:0000256|HAMAP-Rule:MF_00568};
GN   OrderedLocusNames=Tfu_0575 {ECO:0000313|EMBL:AAZ54613.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54613.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC       dihydroxyacetone phosphate to form quinolinate.
CC       {ECO:0000256|HAMAP-Rule:MF_00568, ECO:0000256|SAAS:SAAS00883591}.
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:0000256|HAMAP-Rule:MF_00568,
CC         ECO:0000256|SAAS:SAAS01116083};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00568};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00568};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from iminoaspartate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00568,
CC       ECO:0000256|SAAS:SAAS00883494}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00568}.
CC   -!- SIMILARITY: Belongs to the quinolinate synthase A family. Type 2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00568}.
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DR   EMBL; CP000088; AAZ54613.1; -; Genomic_DNA.
DR   RefSeq; WP_011291022.1; NC_007333.1.
DR   STRING; 269800.Tfu_0575; -.
DR   EnsemblBacteria; AAZ54613; AAZ54613; Tfu_0575.
DR   KEGG; tfu:Tfu_0575; -.
DR   eggNOG; ENOG4105D0I; Bacteria.
DR   eggNOG; COG0379; LUCA.
DR   HOGENOM; HOG000222770; -.
DR   KO; K03517; -.
DR   OMA; LWAPDRH; -.
DR   OrthoDB; 613347at2; -.
DR   BioCyc; TFUS269800:G1G4Q-585-MONOMER; -.
DR   UniPathway; UPA00253; UER00327.
DR   Proteomes; UP000000434; 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_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;
DR   PRODOM; Q47SF4.
DR   SWISS-2DPAGE; Q47SF4.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00883558};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00568, ECO:0000256|SAAS:SAAS00883499};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00883597};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00883634};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00883480};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00568,
KW   ECO:0000256|SAAS:SAAS00883490}.
FT   BINDING      34     34       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
FT   BINDING      51     51       Iminoaspartate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00568}.
FT   BINDING     122    122       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
FT   BINDING     139    139       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
FT   BINDING     209    209       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
FT   BINDING     237    237       Iminoaspartate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00568}.
SQ   SEQUENCE   332 AA;  35906 MW;  CCC644AC09C7B1C6 CRC64;
     MATVTTSADT MTRQEWAAEV RRLAKERDAV ILAHNYQRPE IQDVADYTGD SLALSRLAAT
     VEASTIVFCG VHFMAETAKL LSPEKTVLLP DPAAGCSLAD TITAEDVRAW RAEHPDAVAV
     AYVNTTAAVK AEVDICCTSS NAADVIRSIP EDREILFLPD QFLGAHVKRV TGRDNIHVWM
     GECHVHAGID GHTLRQRVEA EPDAELYVHP ECGCATSALY LASSGMVPEE RVKVLSTGGM
     LRAAEKTTAR KVLIATETGM LHQLRAANPS TVFEPVNSRA ECHYMKMITA EKLLASLRDG
     TTEITVPEDV AARARASVER MIAIGSPSRG GE
//

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