ID A0A0D1YIY2_9PEZI Unreviewed; 783 AA.
AC A0A0D1YIY2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=PV09_07597 {ECO:0000313|EMBL:KIW00837.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW00837.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW00837.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW00837.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) 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; KN847559; KIW00837.1; -; Genomic_DNA.
DR RefSeq; XP_016210706.1; XM_016361380.1.
DR AlphaFoldDB; A0A0D1YIY2; -.
DR STRING; 253628.A0A0D1YIY2; -.
DR GeneID; 27315570; -.
DR VEuPathDB; FungiDB:PV09_07597; -.
DR HOGENOM; CLU_006714_2_2_1; -.
DR InParanoid; A0A0D1YIY2; -.
DR OrthoDB; 3266779at2759; -.
DR Proteomes; UP000053259; 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; cd01578; AcnA_Mitochon_Swivel; 1.
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:UP000053259};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 67..503
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 583..711
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 518..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 85571 MW; 08EB2C2201CDB887 CRC64;
MLSSTSRLAS RRLLGRRGFA SVVDTSKLDR KVEMNNWEKG HYINYKKMYE NLQVVRSRLN
RPLTYGEKIL YSHLDNPHEQ DIERGVSYLK LRPDRVACQD ATAQMAILQF MSAGMPSVAT
PTTVHCDHLI EAQVGGPQDL ARAKEINREV YDFLSSSCAK YNIGFWRPGS GIIHQIILEN
YAFPGGLLIG TDSHTPNAGG LGMVAIGVGG ADAVDVMANL PWELKAPKYI GVKLTGKLSG
WTAPKDIILK VAGILTVKGG TGAIVEYFGP GTESLSATGM GTICNMGAEI GATTSLFPFN
DRMYDYLVAT KRKAIGDLAR EYAAELHEDE GAEYDQLIEI DLNTLEPHIN GPFTPDLATP
ISKFKDAVKE NGWPEELKVG LIGSCTNSSY EDMSRAASIA TDAMEHGLKS KAIFTVTPGS
EQIRATIERD GQMKTFEEFG GMVLANACGP CIGQWDRKDV KKGEPNSIIS SYNRNFTGRN
DANPATHAFV TSPDLVVAMS IAGKLTFNPL TDTLKDKDGK EFKLKEPSGD GLPKNGYDAG
ENTYQAPPAD RESVQVKVSP TSDRLQILEK FEPWDGKDAL NIPILIKAKG KTTTDHISMA
GPWLKYRGHL DNISNNMLIG AVNAANGEAN KVKNQITGEW GPVPATARDY KQKGIKWVVI
GDWNYGEGSS REHAALEPRH LGGLAIITRS FARIHETNLK KQGMLPLTFT NPEDYDRINP
DDKVDLLCTE LAVGKPITLR VHPADGGKPF DIKLSHTFNE GQIEWFKNGS ALNTMAKQAA
AKA
//
