ID A0A0A8L506_9SACH Unreviewed; 781 AA.
AC A0A0A8L506;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=KLDO_g1625 {ECO:0000313|EMBL:CDO93324.1};
OS Kluyveromyces dobzhanskii CBS 2104.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO93324.1, ECO:0000313|Proteomes:UP000031516};
RN [1] {ECO:0000313|EMBL:CDO93324.1, ECO:0000313|Proteomes:UP000031516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA Nystedt B., Astrom S.;
RT "The genome of Kluyveromyces dobzhanskii.";
RL Submitted (MAR-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDO93324.1}.
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DR EMBL; CCBQ010000022; CDO93324.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A8L506; -.
DR OrthoDB; 3266779at2759; -.
DR Proteomes; UP000031516; 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 Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 65..502
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 581..710
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 781 AA; 84952 MW; 61BABEE4B056E13E CRC64;
MLCARVALKK QGVRHLATAV NGSLTRDSKV FQNLLENHSF INYKENIDFV NIVRERLGRP
LTYAEKILYG HLDDPHGQEI ERGISYLKLR PDRVACQDAT AQMAILQFMS AGLPEVARPV
TVHCDHLIQA QVGGEKDLKR AIDINKEVYD FLSTATAKYN MGFWKPGSGI IHQIVLENYA
FPGALIIGTD SHTPNAGGLG QLAIGVGGAD AVDVMSNLAW ELKAPKIMGV KLTGRMNGWT
SPKDIILKLA GITTVKGGTG KIVEYFGEGI DTFSATGMGT ICNMGAEIGA TTSVFPYNQS
MVDYLDATGR GKIAEFAKLY QKDLLSADEG AEYDEVIEID LNTLEPYVNG PFTPDLATPI
SKLKDVAVEN NWPLEVKVGL IGSCTNSSYE DMSRAASVVK DAATHGLKSK SIFTVTPGSE
QIRATIARDG QLETFTEFGG TVLANACGPC IGQWDRQDIK KGDKNTIVSS FNRNFTARND
GNPDTHSFVA SPEITTAFAI AGDLRFNPLT DSLKDKNGNE FKLKPPTGVG LPVKGYDPGE
NTYQAPPADR SSVTVQVSPE SDRLQLLKPF KAWDGKDALD MPILIKSLGK TTTDHISMAG
PWLKYRGHLQ NISNNYMIGA INAENKKANC VKHHYTGEYD GVPNTAAKYR DEGIKWVVIG
GENFGEGSSR EHAALEPRYL GGFAIITKSF ARIHETNLKK QGLLPLNFAE PAAYDRINPD
DTIDILGLTT LAPGKNLTMR VHPKDGAAWD TPLSHTFNAE QIEWFKAGSA LNKLANAKKG
N
//
