位置:首页 > 蛋白库 > LYS4_ASHGO
LYS4_ASHGO
ID   LYS4_ASHGO              Reviewed;         686 AA.
AC   Q75DX9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Homoaconitase, mitochondrial;
DE            EC=4.2.1.36;
DE   AltName: Full=Homoaconitate hydratase;
DE   Flags: Precursor;
GN   Name=LYS4; OrderedLocusNames=ABL106C;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
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., Poehlmann 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]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 357.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
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   -!- FUNCTION: Catalyzes the reversible hydration of cis-homoaconitate to
CC       (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for
CC       lysine biosynthesis. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-homoisocitrate = cis-homoaconitate + H2O;
CC         Xref=Rhea:RHEA:15485, ChEBI:CHEBI:15377, ChEBI:CHEBI:15404,
CC         ChEBI:CHEBI:58174; EC=4.2.1.36;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 3/5.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000305}.
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; AE016815; AAS50665.2; -; Genomic_DNA.
DR   RefSeq; NP_982841.2; NM_208194.2.
DR   AlphaFoldDB; Q75DX9; -.
DR   SMR; Q75DX9; -.
DR   STRING; 33169.AAS50665; -.
DR   EnsemblFungi; AAS50665; AAS50665; AGOS_ABL106C.
DR   GeneID; 4618921; -.
DR   KEGG; ago:AGOS_ABL106C; -.
DR   eggNOG; KOG0453; Eukaryota.
DR   HOGENOM; CLU_006714_3_1_1; -.
DR   InParanoid; Q75DX9; -.
DR   OMA; VMIRPEH; -.
DR   UniPathway; UPA00033; UER01027.
DR   Proteomes; UP000000591; Chromosome II.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0004409; F:homoaconitate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR   CDD; cd01674; Homoaconitase_Swivel; 1.
DR   Gene3D; 3.20.19.10; -; 1.
DR   Gene3D; 3.30.499.10; -; 2.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR004418; Homoaconitase_mito.
DR   InterPro; IPR039386; Homoaconitase_swivel.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR00139; h_aconitase; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Iron; Iron-sulfur; Lyase; Lysine biosynthesis;
KW   Metal-binding; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..17
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..686
FT                   /note="Homoaconitase, mitochondrial"
FT                   /id="PRO_0000247915"
FT   BINDING         337
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         401
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         404
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   686 AA;  72448 MW;  3F05330751A6735D CRC64;
     MRVVRCVRRF SASRAVSGQN TTEKIVQAHA VGLRPGHRVA SGDYVSIRPA HCMSHDNSWP
     VALKFMGLGA TRVHDARQVV CTLDHDVQNR SEKNLAKYRN IELFAAQQGV DFYPARRGIG
     HQIMVEEGYA FPLGLTVASD SHSNTYGGVG ALGTPVVRTD AAAIWATGQT WWQVPPVARV
     ELTGELPAGV SGKDAIVALC GVFGRDEVLN HAVEFAGPGV ARLTVEQRLT VANMTTEWGA
     LSGLFPVDGV LLDWYREQVA RAPAGHARLT AARVDALAER AAAMQPDTDA RYAKQLTLDL
     SSLTHYVSGP NSVKVARPIA ELAPQQLRID KAYLLSCTNG RLEDLEAAAA VLRADGSVRQ
     VAPGVEFYIA AASAEVEAQA RARGTWDVLL SAGCIPLPSG CGPCIGLGKG LLEAGEVGIS
     ATNRNFRGRM GSKDAEAYLA SPAVVAASAV LGRIAAPCEV LGLSPPAAPA VRASVAQCGA
     PAAADGAAAA VEVLPGFPRA ITGELVLCDA DNINTDGIYP GKYTYEDDIP RETMARVCME
     NYDLDFQHNV HAGDIVVGGY NFGTGSSREQ AATALLAKGV PLVVAGSFSN TFSRNAINNA
     LLTLELPALL QLLRERYADA PSQATRRTGV FLTWDVAAAT VTVTVGSPTG ERVLHQRVGE
     FSANLQEIIV KGGLEGWVKH ALAQSA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024