ID   A0A238FA70_9BASI        Unreviewed;       769 AA.
AC   A0A238FA70;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|ARBA:ARBA00015940, ECO:0000256|RuleBase:RU362107};
DE            Short=Aconitase {ECO:0000256|RuleBase:RU362107};
DE            EC=4.2.1.- {ECO:0000256|RuleBase:RU362107};
GN   ORFNames=BQ2448_1024 {ECO:0000313|EMBL:SCV68903.1};
OS   Microbotryum intermedium.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV68903.1, ECO:0000313|Proteomes:UP000198372};
RN   [1] {ECO:0000313|Proteomes:UP000198372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jeantristanb JTB J.-T., Ricardo R.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
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|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU362107}.
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DR   EMBL; FMSP01000003; SCV68903.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238FA70; -.
DR   STRING; 269621.A0A238FA70; -.
DR   OrthoDB; 3266779at2759; -.
DR   Proteomes; UP000198372; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd01584; AcnA_Mitochondrial; 1.
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:SF3; ACONITATE HYDRATASE, 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:UP000198372};
KW   Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT   DOMAIN          68..490
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          569..698
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   769 AA;  82834 MW;  25897300B788A60A CRC64;
     MVLIPSARQM GLRAPQLSRS LATPASSIGA TKVAMSLFEK DKYINYQRIE DNLAVVRQRL
     ERKLTLSEKV LYGHLDNPHD ADIRRGASYL KLRPDRVACQ DATAQMALLQ FMSAGLPTVA
     VPTTVHCDHL IEAQVGGAKD LARANDINKE VYDFLATCTA KQIILENYAF PGGLMIGTDS
     HTPNAGGLGM IAVGVGGADA VDVIADLPWE LKCPKTIGVK LTGKIGGWTT PKDVILKVAG
     ILTVKGGTGA IVEYFGEGVN SLSCTGMATI CNMGAEIGAT TSLFPYNSRM GDYLDATKRP
     EIRKYAEAFQ HNLRADEGAD YERVIEINLS ELEPHINGPY TPDLATPLSK FAEAVKANDW
     PEKLSVGLIG SCTNSSYEDM SRSASIAKEA AEHGLKAKSG FTITPGSEQI RATIERDGQI
     KVLEDAGGLV LANACGPCIG QWDRRDVPKG TKNSIITSYN RNFTARNDAN TATHAFVASP
     DLVTAMVFAG SMTFNPLTDS LKGADGKEFK FSDPTGKELP PLGYDPGQDT YQAPPADRAS
     VNVIVSPTSD RLQILKPFKK WNGEDPTDMP VLIKAVGKCT TDHISAGGPW LKYRGHLENI
     SQNCLIGAIN AANGEANKVQ NLLTGEWGAV PKVAAEYRDA GVPWVVIGDE NYGEGSSREH
     AALEPRFLGG AAVITRSFAR IHETNLKKQG MLPLNFKNPA DYDKVQPDDK VDLIGVKDLA
     EGSTVKMVLK HKDGKTETIE LTHTFNADQI RWHRAGSALN AMAEAKASQ
//