(data stored in ACNUC6288 zone)

SWISSPROT: LYS4_DEBHA

ID   LYS4_DEBHA              Reviewed;         688 AA.
AC   Q6BM98;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 87.
DE   RecName: Full=Homoaconitase, mitochondrial;
DE            EC=4.2.1.36;
DE   AltName: Full=Homoaconitate hydratase;
DE   Flags: Precursor;
GN   Name=LYS4; OrderedLocusNames=DEHA2F07238g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Catalyzes the reversible hydration of cis-homoaconitate
CC       to (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate
CC       pathway for lysine biosynthesis. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1R,2S)-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;
CC         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}.
DR   EMBL; CR382138; CAG89007.1; -; Genomic_DNA.
DR   RefSeq; XP_460673.1; XM_460673.1.
DR   STRING; 4959.XP_460673.1; -.
DR   PRIDE; Q6BM98; -.
DR   EnsemblFungi; CAG89007; CAG89007; DEHA2F07238g.
DR   GeneID; 2903254; -.
DR   KEGG; dha:DEHA2F07238g; -.
DR   HOGENOM; HOG000173778; -.
DR   InParanoid; Q6BM98; -.
DR   KO; K01705; -.
DR   OMA; IAGPGWY; -.
DR   OrthoDB; 265826at2759; -.
DR   UniPathway; UPA00033; UER01027.
DR   Proteomes; UP000000599; Chromosome F.
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; -; 1.
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; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BM98.
DR   SWISS-2DPAGE; Q6BM98.
KW   Amino-acid biosynthesis; Complete proteome; Iron; Iron-sulfur; Lyase;
KW   Lysine biosynthesis; Metal-binding; Mitochondrion; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1     19       Mitochondrion. {ECO:0000255}.
FT   CHAIN        20    688       Homoaconitase, mitochondrial.
FT                                /FTId=PRO_0000247923.
FT   METAL       346    346       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL       406    406       Iron-sulfur (4Fe-4S). {ECO:0000250}.
FT   METAL       409    409       Iron-sulfur (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   688 AA;  74358 MW;  B1E0A2C936163F89 CRC64;
     MALLYLSTRS SLKKTGARCL SSSSILYRGQ NLTEKIVQKY AVGLADDKKV FSGDYVTIKP
     AHCMSHDNSW PVATKFMGLG ATNVHDNRQI VCTLDHDVQN KSEKNLEKYH NIENFAKEQG
     IDFYPAGRGI GHQIMIEEGY AYPLNLTVAS DSHSNTYGGI GSLGTPIVRT DAASIWATGQ
     TWWQIPPVAK VELVGQLPKG ATGKDIIVAL CGIFNNDEVL NHAIEFTGEG VKNLSVDYRL
     TIANMTTEWG ALSGLFPVDE TLVNFYDERV KKLPQPHPRV NENTVKNLSE NKVNSDNDAV
     YAKHLVVDLS SLSPYISGPN SVKVSTSLHD LSKQNIKINK AYLVSCTNSR LSDIKAAADI
     IKGHKVAEGV EFYVAAASSN VQKDAEAIGA WQDIIDAGAK PLPAGCGPCI GLGTGLLEDG
     EVGISATNRN FKGRMGSKDA LAYLASPEVV AASAVLGKIG GPEELQGNPV PTNPEIVRSI
     TSNESTETVD PDASGSSVDV LDGFPQSIEG ELILCDADNI NTDGIYPGKY TYQDDIPRSK
     MAEVCMENYD SEFKQKTKAG DIIISGYNFG TGSSREQAAT AILARDMKLV VAGSFGNIFS
     RNSINNALLT LEIPALINKL REKYAQSNEL TIRTGWFLKW DVTKNQVTVS DSEGNLILTQ
     KVGELGTNLQ DIIVKGGLEG WVKAQLKN
//

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