(data stored in SCRATCH zone)

SWISSPROT: Q750K8_ASHGO

ID   Q750K8_ASHGO            Unreviewed;       557 AA.
AC   Q750K8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 103.
DE   RecName: Full=Isocitrate lyase {ECO:0000256|PIRNR:PIRNR001362};
GN   ORFNames=AGOS_AGL057W {ECO:0000313|EMBL:AAS54433.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54433.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54433.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001362-3};
CC       Note=Can also use Mn(2+) ion. {ECO:0000256|PIRSR:PIRSR001362-3};
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000256|PIRNR:PIRNR001362}.
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; AE016820; AAS54433.2; -; Genomic_DNA.
DR   RefSeq; NP_986609.2; NM_211671.2.
DR   STRING; 33169.AAS54433; -.
DR   EnsemblFungi; AAS54433; AAS54433; AGOS_AGL057W.
DR   GeneID; 4622908; -.
DR   KEGG; ago:AGOS_AGL057W; -.
DR   HOGENOM; HOG000238475; -.
DR   InParanoid; Q750K8; -.
DR   KO; K01637; -.
DR   OMA; TVPHADF; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0004451; F:isocitrate lyase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046421; F:methylisocitrate lyase activity; IBA:GO_Central.
DR   GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IBA:GO_Central.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; -; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR006254; Isocitrate_lyase.
DR   InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR21631; PTHR21631; 1.
DR   Pfam; PF00463; ICL; 1.
DR   PIRSF; PIRSF001362; Isocit_lyase; 2.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR01346; isocit_lyase; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750K8.
DR   SWISS-2DPAGE; Q750K8.
KW   Lyase {ECO:0000256|PIRNR:PIRNR001362};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   REGION          116..118
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   REGION          221..222
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   REGION          440..444
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   ACT_SITE        220
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   METAL           182
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         257
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         475
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   557 AA;  61359 MW;  8578761965EFBC89 CRC64;
     MASVWRRSLK TLSSYPRPSG SSAKRFVEEQ TTELEQLWSS PRFQEITRPY TPLDVVKHRG
     SLGRVGYASS VQAERLHDLL EDKFHKREAV STLGVIDPVQ MTQLARCEGI EAAYVSGWAC
     SSTMVGSTNE VSPDFGDYPY DTVPNQVERI FRAQQMHDRK AFLADGAEGR ASTDYLKPII
     ADGDMGHGGS TTVMKLAKLF AEKGAAAIHL EDQMHGGKRC GHLGGAVLAP TYVHISRLIA
     TRLQWDIMGT QNLLIARTDS ANAKLIASSS DPRDHEFILG TTQPAAQPWA ELVLDMEAAG
     CTAQEIAAAE QEWFDECPLL TFDQAAEQQL SSSEYGAYGA RKKELCSQLG RPYLALREMR
     HIAEAVAPHK SVNFDWDAPR TREGHHMLHG CMELAVRRTL AFAPYSDLLW LETKTPDLRQ
     ASAFAAAIHR AYPHAKLVYN LSPSFNWTAH GYDDRQLRAF IPSLAAAGFV LQLVSLAGLH
     SDALAFWQLA AAFPADGMLA YVQHVQAPER RSGCDVLLHQ RWSGVDYVDS LGNLVQNGAS
     SHTRGAGGDS FTESQFQ
//

If you have problems or comments...

PBIL Back to PBIL home page