ID   LYS4_CANPA              Reviewed;         688 AA.
AC   Q2HZ33;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Homoaconitase, mitochondrial;
DE            EC=4.2.1.36;
DE   AltName: Full=Homoaconitate hydratase;
DE   Flags: Precursor;
GN   Name=LYS4;
OS   Candida parapsilosis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CBS 604;
RA   Gavenciakova B., Kosa P., Nosek J.;
RT   "Candida parapsilosis LYS4 gene.";
RL   Submitted (JAN-2006) 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: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; DQ359726; ABC94604.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2HZ33; -.
DR   SMR; Q2HZ33; -.
DR   CGD; CAL0000151989; CPAR2_500690.
DR   VEuPathDB; FungiDB:CPAR2_500690; -.
DR   UniPathway; UPA00033; UER01027.
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.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Iron; Iron-sulfur; Lyase; Lysine biosynthesis;
KW   Metal-binding; Mitochondrion; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..688
FT                   /note="Homoaconitase, mitochondrial"
FT                   /id="PRO_0000247920"
FT   REGION          468..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         335
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         395
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         398
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   688 AA;  74577 MW;  9130D4C19E7BC84E CRC64;
     MRLHLHRFIS TSTPLRSGQN LTEKIVQKYA VNLPPNKLVH TGDYVTIKPA HCMSHDNSWP
     VATKFMGLGA KRVKDNRQIV CTLDHDVQNK TEKNLAKYAN IERFAKEQGI DFYPAGRGIG
     HQIMIEEGYA FPLNLTVASD SHSNTYGGVG SLGTPIVRTD AASIWATVQT WWQIPPVAKV
     ELKGNLQNGV TGKDIIVALC GVFNNDEVLN HAIEFVGDGV ENLPIDYRLT IANMTTEWGA
     LSGLFPIDDK LIEFYEGRLQ KLGPNHPRIN KDTIEALRRG SLASDEDAKY AKHLVIDLNT
     LSPYVSGPNS VKVSNPLSKL SQDNIAINKA YLVSCTNSRL SDIQAAADVL KGHKVHPNVE
     FYVAAASSLV QQDAEAAGAW QTIIDAGAKP LPAGCGPCIG LGTGLLKDGE VGISATNRNF
     KGRMGSKDAL AYLASPEVVA ASAVLGKIGA PEEIDGKPVN ASPEIVKSID LPKSSGNTGA
     TSEEPISEDD TSEASVEVLP GFPKSIQGEL ILCNADNINT DGIYPGKYTY QDDISREQMA
     EVCMENYDPE FKTKTKSDDI IISGYNFGTG SSREQAATCI LARGMKLVVA GSFGNIFSRN
     SINNALLTLE IPELIEKLRV KYDGVNELTI RTGWFLKWDV TKALVTVADL DGEVILQQKV
     GELGTNLQDI IVKGGLEGWV KSELQKEQ