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Database: UniProt
Entry: A0A135THI1_9PEZI
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ID   A0A135THI1_9PEZI        Unreviewed;       792 AA.
AC   A0A135THI1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Homoaconitase, mitochondrial {ECO:0000256|ARBA:ARBA00021560, ECO:0000256|RuleBase:RU362038};
DE            EC=4.2.1.36 {ECO:0000256|ARBA:ARBA00012022, ECO:0000256|RuleBase:RU362038};
DE   AltName: Full=Homoaconitate hydratase {ECO:0000256|ARBA:ARBA00032706, ECO:0000256|RuleBase:RU362038};
GN   ORFNames=CNYM01_07897 {ECO:0000313|EMBL:KXH47646.1};
OS   Colletotrichum nymphaeae SA-01.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH47646.1, ECO:0000313|Proteomes:UP000070054};
RN   [1] {ECO:0000313|EMBL:KXH47646.1, ECO:0000313|Proteomes:UP000070054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA-01 {ECO:0000313|EMBL:KXH47646.1,
RC   ECO:0000313|Proteomes:UP000070054};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible hydration of cis-homoaconitate to
CC       (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for
CC       lysine biosynthesis. {ECO:0000256|ARBA:ARBA00003422,
CC       ECO:0000256|RuleBase:RU362038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-homoisocitrate = cis-homoaconitate + H2O;
CC         Xref=Rhea:RHEA:15485, ChEBI:CHEBI:15377, ChEBI:CHEBI:15404,
CC         ChEBI:CHEBI:58174; EC=4.2.1.36;
CC         Evidence={ECO:0000256|ARBA:ARBA00029338,
CC         ECO:0000256|RuleBase:RU362038};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU362038};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000256|RuleBase:RU362038};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 3/5.
CC       {ECO:0000256|ARBA:ARBA00005106, ECO:0000256|RuleBase:RU362038}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC       ECO:0000256|RuleBase:RU362038}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|RuleBase:RU362038}.
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:KXH47646.1}.
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DR   EMBL; JEMN01001110; KXH47646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135THI1; -.
DR   UniPathway; UPA00033; UER01027.
DR   Proteomes; UP000070054; 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:0004409; F:homoaconitate hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniRule.
DR   CDD; cd01674; Homoaconitase_Swivel; 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; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR004418; Homoaconitase_mito.
DR   InterPro; IPR039386; Homoaconitase_swivel.
DR   NCBIfam; TIGR00139; h_aconitase; 1.
DR   PANTHER; PTHR43822:SF2; HOMOACONITASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 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   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362038};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362038};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362038};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362038};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154,
KW   ECO:0000256|RuleBase:RU362038};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362038};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU362038};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW   ECO:0000256|RuleBase:RU362038}.
FT   DOMAIN          110..521
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          593..716
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   792 AA;  85202 MW;  8FBE2E187A36F786 CRC64;
     MLPIRRTVAL HAARSCRRSL LQRQLPSRSI RPSFYTTTTR PRQYAFHSQL ENAATATDFL
     YTTAPKVENP QTLTEKIVQR HSLGLAPGKK VRAGDYVTLS PAHQAYNWEG KCMSHDNTAP
     ISNKFVSIGA TKIHNPSQLV WTLDHDVQNK SEANLKKYKK IEDLGKQHGV VFYPAGRGIG
     HQIMVEEGYA WPGTLAVASD SHSNHYGGIG CLGTAVVRTD AAAIWATGRT WYQVPPIAKI
     TLTGVKPPGV TGKDIIVALC GLFNKDDVLN HALEFTGSEE TMRSIPVDER ITVANMSTEW
     GALSALFPID QTLERWLRAK ATTAAMLNTD AAVKGRWTHE RIDELLENPL TADAGATYAK
     SLYLNLETLS PFVAGPNSVK VATPLKDLEA QNIKIDKAYL VSCTNSRASD IAAAARVFRE
     AAKDGQPAKI APGVSFYLAA ASTVEQAAAE EAGDWQTLID AGCSVLPSGC GPCIGLGTGL
     LEPGENGISA SNRNFKGRMG STEAKAYLAS PEVVAASALN GKIAGPGWYQ QPQGVDKVII
     GEGVGDITAD IAMSIDDALD QLIAQADSMI AESEMGVAGA AAPAAEEPAA AAESEEDSLT
     EVLPGFPEKV EGEIIFCDQD NMNTDGIYPG KYTYQDNVSV EKMAEVCMEN YDTSFRDIAK
     AGDILVSGFN FGTGSSREQA ATAILAKKIP LVVSGSFGNI FSRNSINNAL MGVEVPKLVQ
     RLRETFKNEG EDKVLTRRTG WKLCWDLRRS KVIVTEGSGE SWSVKVGELP PNVQEVIAKG
     GLEAWVKAEI EK
//
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