ID   Q6C5V2_YARLI            Unreviewed;       790 AA.
AC   Q6C5V2;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|RuleBase:RU362107};
DE            Short=Aconitase {ECO:0000256|RuleBase:RU362107};
DE            EC=4.2.1.- {ECO:0000256|RuleBase:RU362107};
GN   ORFNames=YALI0_E14949g {ECO:0000313|EMBL:CAG79553.1};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG79553.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG79553.1, ECO:0000313|Proteomes:UP000001300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., 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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU362107};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000256|RuleBase:RU362107};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC       ECO:0000256|RuleBase:RU362107}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|RuleBase:RU362107}.
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DR   EMBL; CR382131; CAG79553.1; -; Genomic_DNA.
DR   RefSeq; XP_503960.1; XM_503960.1.
DR   AlphaFoldDB; Q6C5V2; -.
DR   STRING; 284591.Q6C5V2; -.
DR   EnsemblFungi; CAG79553; CAG79553; YALI0_E14949g.
DR   GeneID; 2911538; -.
DR   KEGG; yli:YALI0E14949g; -.
DR   VEuPathDB; FungiDB:YALI0_E14949g; -.
DR   HOGENOM; CLU_006714_2_2_1; -.
DR   InParanoid; Q6C5V2; -.
DR   OMA; KWPETFG; -.
DR   OrthoDB; 3266779at2759; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR   GO; GO:0003994; F:aconitate hydratase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 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; IPR015932; Aconitase_dom2.
DR   InterPro; IPR006248; Aconitase_mito-like.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   NCBIfam; TIGR01340; aconitase_mito; 1.
DR   PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR   PANTHER; PTHR43160:SF2; HOMOCITRATE DEHYDRATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362107};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362107};
KW   Lyase {ECO:0000256|RuleBase:RU362107};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362107};
KW   Mitochondrion {ECO:0000256|RuleBase:RU362107};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW   Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT   DOMAIN          65..505
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          586..714
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   790 AA;  85638 MW;  C1E2F9687D3DDD0E CRC64;
     MLRSARFCQA RFSAIKARGL ATTANASGLS VPADFKTRTP PYAELINRLD QVKKIINRND
     LTLAEKILYS HLHNPEETPS ITRGDTYLKL NPDRVAMQDA SAQMALLQFM TCGLPSTAVP
     ASIHCDHLIV GRDGADDDLT RSIATNQEVF DFLQQCAEKY GIQFWGPGSG IIHQIVLENF
     SVPGLMMLGT DSHTPNAGGL GAIAIGVGGA DAVDALTGTP WELKAPKILG VKLTGKLSGW
     ASPKDVITHL AGKLTVRGGT GNIIEYHGEG VDSLSCTGMA TICNMGAEVG ATTSTFPFTE
     SMRRYLEATG RAPIAAAAAA ARDRGFLAAD EGAQYDEVVE VNLSELEPCI NGPFTPDLAT
     PLSKYSTKVT SEKWPDTVSA GLIGSCTNSS YEDMTRVASL VEQARDNGLE AKIPFFITPG
     SEQIRATIKK DGLTDVFESA GAVVLANACG PCIGQWDRTD ETKPGEFNSI FTSFNRNFRA
     RNDGNPETMN FLTSPEIVTA MIYSGDAHFN PMTDSITTKD GKEFKFQPPK GTELPEEFAK
     GRPEFYPEAA PQPHPEVNVT VSPDSERLQL LEPFEPFNNQ ELKLSVLMKV EGKCTTDHIS
     AAGAWLKYKG HLENISYNTL IGALNKETQK VNHTIDAADG SEQSIPDLMI KWKEQGKPWI
     VVAEHNYGEG SAREHAALSP RFLGGQAILV KSFARIHETN LKKQGMLPLT FENEADYDKI
     QACDTLETLD LLDMLEKGGD NGGFVQMRAT KSDGSTYDFR ARHTMSADQV DFFKAGSAIN
     FIGAQKAANK
//