ID   LYS4_CHAGB              Reviewed;         797 AA.
AC   Q2GN26;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Homoaconitase, mitochondrial;
DE            EC=4.2.1.36;
DE   AltName: Full=Homoaconitate hydratase;
DE   Flags: Precursor;
GN   Name=LYS4; ORFNames=CHGG_10628;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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:0000250}.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 3/5.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; CH408035; EAQ84224.1; -; Genomic_DNA.
DR   RefSeq; XP_001228555.1; XM_001228554.1.
DR   AlphaFoldDB; Q2GN26; -.
DR   SMR; Q2GN26; -.
DR   STRING; 38033.XP_001228555.1; -.
DR   EnsemblFungi; EAQ84224; EAQ84224; CHGG_10628.
DR   GeneID; 4396424; -.
DR   eggNOG; KOG0453; Eukaryota.
DR   HOGENOM; CLU_006714_3_1_1; -.
DR   InParanoid; Q2GN26; -.
DR   OMA; VMIRPEH; -.
DR   OrthoDB; 265826at2759; -.
DR   UniPathway; UPA00033; UER01027.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0004409; F:homoaconitate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR   CDD; cd01674; Homoaconitase_Swivel; 1.
DR   Gene3D; 3.20.19.10; -; 1.
DR   Gene3D; 3.30.499.10; -; 2.
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   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; SSF53732; 1.
DR   TIGRFAMs; TIGR00139; h_aconitase; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Iron; Iron-sulfur; Lyase; Lysine biosynthesis;
KW   Metal-binding; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..47
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..797
FT                   /note="Homoaconitase, mitochondrial"
FT                   /id="PRO_0000247921"
FT   BINDING         404
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         471
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         474
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   797 AA;  85257 MW;  251AAFF95459BD27 CRC64;
     MVARFVPSAM TVLVARRGLA MASTRRGWRG LAVNLKPAAG RQWRQAYSTT PVRQNALHSE
     IEAQAASPFA APGTRVQNPQ TLTEKIVQRY AIGLPPGKKV KAGDYVTISP AQCMTHDNSW
     PVVTKFTSIG ATKIHNNRQV VVTLDHDVQN TSESNLKKYK NIENFARQHG VDFYPAGRGI
     GHQIMIEEGY AWPGTLTVAS DSHSNMYGGV AALGTPVVRT DAASIWATGQ TWWQIPPIAK
     VTFTGVLPRG VTGKDVIIAL CALFNQDEVL NHAIEFTGSD LTLSSLPIDD RLTISNMTTE
     WGAVAGIFPI DSTLKSWLRA KATVSAMLNP DLGGKARITH DKIEELFRDP PKPDLGATYA
     KSLYLNLSTL SPFVAGPNSV KVATPVKDLE AQNIKINKAY LVSCTNSRAS DIAAAANVFR
     EAANGGPIPK VAPGVEFYIS AASLPEQEIA EQAGDWRVLL DAGCIENPAS CNACIGLGRG
     LLQPGDVGIS ASNRNWNGRM GSPQAKAYLA SPEVVAASAL KGEIAGPGWY EKPEGVEKVI
     IGEGTGDLEA DRAVSIADAL ESLVAQAESM ISSAEKSLES SPAAATGAVG NAMADATADQ
     AGEEGLIDIL PGFPEKVSGE IVFCDSDNIN TDGIYPGKYT YQDDITRDTM AQVVMENYDR
     SFASLAKPGD ILVAGFNFGC GSSREQAATA ILAKGIPLVV AGSFGNIFSR NSINNALMGV
     EVPRLVKRLR EEFGEKVPTR RTGWRFEWDV RRSKVTVTEG EGGETWSQKV GDLPPNVQEI
     IAVGGLEKWV KHRISQA