(data stored in SCRATCH zone)

SWISSPROT: D1YUZ3_METPS

ID   D1YUZ3_METPS            Unreviewed;       300 AA.
AC   D1YUZ3;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 48.
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   ECO:0000313|EMBL:BAI60265.1};
GN   OrderedLocusNames=MCP_0193 {ECO:0000313|EMBL:BAI60265.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60265.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC       dihydroxyacetone phosphate to form quinolinate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00568};
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 from
CC       iminoaspartate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00568}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP011532; BAI60265.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0193; -.
DR   EnsemblBacteria; BAI60265; BAI60265; MCP_0193.
DR   KEGG; mpd:MCP_0193; -.
DR   PATRIC; fig|304371.9.peg.200; -.
DR   eggNOG; arCOG04459; Archaea.
DR   eggNOG; COG0379; LUCA.
DR   HOGENOM; HOG000222770; -.
DR   KO; K03517; -.
DR   OMA; LWAPDRH; -.
DR   UniPathway; UPA00253; UER00327.
DR   Proteomes; UP000001882; 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   3: Inferred from homology;
DR   PRODOM; D1YUZ3.
DR   SWISS-2DPAGE; D1YUZ3.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00568};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00568}.
FT   BINDING         22
FT                   /note="Iminoaspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00568"
FT   BINDING         39
FT                   /note="Iminoaspartate; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00568"
FT   BINDING         110
FT                   /note="Iminoaspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00568"
FT   BINDING         127
FT                   /note="Iminoaspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00568"
FT   BINDING         195
FT                   /note="Iminoaspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00568"
FT   BINDING         212
FT                   /note="Iminoaspartate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00568"
SQ   SEQUENCE   300 AA;  32951 MW;  6096288D52D7546B CRC64;
     MTQIVDEIKK LKEARRAVIL AHNYQRGEVQ DIADYVGDSF GLSQKAVEAD AEVIVFCGVD
     FMAESAAILN PGRAVLNPAP EAGCPMARMI TAADVRKLKE QHPGAEVVCY VNSSAEVKAE
     SDVCCTSSNA IKVVNSLKGA EAVFVPDMNL AAYAQKFTSK KIIPWHGYCP THHLITAGDV
     LVAKMEHPGA QVLVHPECRP EVVDLADGVF STDGMIKYAR EATADLIIGT ESGLIHRLKK
     ENPRIRYYPL STYAVCPNMK MTSLVSVRDS LRDMKTQIRV PENIRIRAKK ALDRMLEVGR
//

If you have problems or comments...

PBIL Back to PBIL home page