ID A0A166VDP6_9HYPO Unreviewed; 797 AA.
AC A0A166VDP6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=AAL_01012 {ECO:0000313|EMBL:OAA33547.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:OAA33547.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:OAA33547.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:OAA33547.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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}.
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:OAA33547.1}.
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DR EMBL; AZGY01000001; OAA33547.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166VDP6; -.
DR STRING; 1081109.A0A166VDP6; -.
DR OrthoDB; 3266779at2759; -.
DR Proteomes; UP000078544; 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:UP000078544};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 85..518
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 600..726
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 797 AA; 85353 MW; 864923F8A68F4218 CRC64;
MAILLRLAAR ASGSGASSRC AVAQRRRFSS VKSLPPTYER LFNKYTDVRK ALGTQRLTLA
EKILYSHLDN VQESLLNNTN NGRDVRGKAN LRLKPDRVNM QDASAQMALL QFMSCNLARP
AIPASIHCDH LIVGSKGAED DLEAGIATNK EVFDFLESAA KKYGMDFWPP GAGIIHQTVL
ENYALPGLMM LGTDSHSPNA GGLCTITIGV GGADAVEALV GAPWELKAPK ILGVELTGKL
SNWASPKDVI LKLAGELTVR GGTGFIIEYF GQGVNTLSLT GQSTICNMGA EVGATTSIFP
YTEASARYLQ ATRRGQAVEN IELLQNFPSE GASDDARFQF KADAGAEYDQ VIRIDLSELE
PHINGPFTPD LATPLSQFKT VVKDQQWPEK LSAGLIGSCT NSSYEDMTRV ESLIKEAAQA
GLKPAADFYI TPGSEQIRAT LERDGTLETL ADAGGILLSN ACGPCIGQWK RQDGVEKGTP
NAILTSYNRN FRGRNDGNPE TMNFLASPEI VTAMAFAGST TFNPTTDTLK TPSGDDFKFS
PPHGLEGPRT PFESGVASLG VLSQDADPSV QIAISPSSER LAVLEPFSPF PGSDLSGLRV
LVKVTGKCTT DTISAAGPWL KYKGHLPNIS TNTLNTAINA ETGEVNAAYD LDGSKHTIPE
LAELWKTRGQ EWIVVAEHNY GEGSAREHAA LQPRYLGARV VLTKSFARIH ETNLKKQGVV
PLTFADEADY DKIAAGDSVS TVGLYDMLQS QGKGVVQLKV TKASGEEFLI PTNHAVTKDQ
AGFILAGSAL NLLSKGI
//