ID S3CNT2_OPHP1 Unreviewed; 807 AA.
AC S3CNT2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=F503_00971 {ECO:0000313|EMBL:EPE08188.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE08188.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE08188.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE08188.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU362107}.
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DR EMBL; KE148149; EPE08188.1; -; Genomic_DNA.
DR AlphaFoldDB; S3CNT2; -.
DR STRING; 1262450.S3CNT2; -.
DR VEuPathDB; FungiDB:F503_00971; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR OMA; KWPETFG; -.
DR OrthoDB; 3266779at2759; -.
DR Proteomes; UP000016923; 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 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:UP000016923};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 92..528
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 610..737
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 807 AA; 86538 MW; A52A2E89398320D1 CRC64;
MGPIVLAGRA GALARHIQRP LRALPTTRRL FSTVNDASPI PPVYERLYNN YTTVRRVLGS
ERRLTLTEKI LYSHLDDVET NLLTNTNNGR DIRGKANLQL NPDRVNMQDA SAQMALLQFM
ACNLPQTAIP ASIHCDHLIV GEKGADIDLE AGIGTNGEVF AFLESAARKF GIDFWPPGAG
IIHQTVLENY AIPGLMMLGT DSHTPNAGGL CTIAIGVGGA DAVEALVGAP WELKAPKVLG
VRLTGQLSGW VSPKDVILHL AGLLTVRGGT GFVIEYSGPG VQTLSCTGMA TMTNMGAEVG
ATTSIFPYTA ASARYLESTR RSKQAQDAAN FQQFRGIDAS PTDKDAVFQF AADEGAEYDQ
VIEINLSELE PHINGPFTPD LSIPLSQFRE TVVQEQWPQK LSAGLIGSCT NSSYEDMTRV
ESLLKAAADA GLQPVSDFYV TPGSESIRAT LERDGTLETI DNAGGVLLSN ACGPCIGQWK
RRDGVEKGTS NAIFTSYNRN FRGRNDGNLD TMNFLASPEI VTALAFAGST TFNPLTDSIP
TPDGGEFRFP APHGLEGPPT PFDEGRAAFA ALTQAPDAKI DIAIAPTSER LAILHPFEPF
PDVDLEGLRV LVKVSGKCTT DTISAAGPWL KYKGHLPNIS ANTLNTAVNA ATGEVNVAYD
LDGSKSTIPE LALKWRERNQ PWLVIAEHNY GEGSAREHAA LQPRYLGARI VVVKSFARIH
ETNLKKQGVV PLTFANEADY DRIDAGDIVA TVGLRDMLHA GGQGDVQLKV TKAATGEEFT
IPVKHAVSKD QAGFILAGSA LNMLSKR
//
