ID   LYS4_NEUCR              Reviewed;         784 AA.
AC   Q870W1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Homoaconitase, mitochondrial;
DE            EC=4.2.1.36;
DE   AltName: Full=Homoaconitate hydratase;
DE   Flags: Precursor;
GN   Name=lys-4; ORFNames=B14A21.110, NCU08898;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; BX294091; CAD71225.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA29600.1; -; Genomic_DNA.
DR   RefSeq; XP_958836.1; XM_953743.2.
DR   AlphaFoldDB; Q870W1; -.
DR   SMR; Q870W1; -.
DR   STRING; 5141.EFNCRP00000008828; -.
DR   EnsemblFungi; EAA29600; EAA29600; NCU08898.
DR   GeneID; 3874983; -.
DR   KEGG; ncr:NCU08898; -.
DR   VEuPathDB; FungiDB:NCU08898; -.
DR   HOGENOM; CLU_006714_3_1_1; -.
DR   InParanoid; Q870W1; -.
DR   OMA; VMIRPEH; -.
DR   UniPathway; UPA00033; UER01027.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
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; Reference proteome; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..784
FT                   /note="Homoaconitase, mitochondrial"
FT                   /id="PRO_0000247926"
FT   REGION          572..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         399
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         468
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"
SQ   SEQUENCE   784 AA;  83905 MW;  87BC3D0B803E7779 CRC64;
     MIHPVRRALA VAASRAPRQF LAAASRTTSV RSVRAAAASG SYYSTTSRRL QDAFPSQLEN
     LASSTLPKVV PQVPQTLTEK IVQRYSVGLA PGKKVKSGDY VTLQPHHCMT HDNSWPVAMK
     FMSIGASKIH DNRQVVMTLD HDVQNKSEAN LKKYRQIEEF ANTHGVDFYP AGRGIGHQIM
     VEEGYAWPGT VTVASDSHSN MYGGVGCLGT PMVRTDAASI WATGKTWWQI PPIAKVTFTG
     LLPPGVTGKD VIVALCGLFN NDDVLNHAIE FTGAEETMRS IPVDDRLTIA NMTTEWGALS
     GLFPIDAVLA SWMRAKATVT AMEHPELGDK AKFTHAKIDA LLENPLVADP GATYAKQLYL
     NLSTLSPFVA GPNSVKIATP LKDLEAQNLK LDKAYLVSCT NSRASDIAAA ARVFKDAAAD
     NNGVIPKVAP GVKFYIAAAS LLEQKQAEDS GDWQVLLDAG AEPLPSGCGP CIGLGTGLLE
     PGEIGISASN RNFKGRMGST DAKAYLASPE VVAASALKGK IAGPGWYQKP EGVEKVIIGE
     GNGVVEQDKA MSIEDALDKI IAEAESLIAN AEAGLTPEST SSSSSSSSSS EEESLTEILP
     GFPEAISGEI IFCDADNINT DGIYPGKYTY QDNITPAKMA EVCMENYDAS FGSIARAGDI
     LVTGFNFGCG SSREQAATAI LAKQIPLVVS GSFGNIFSRN SINNALMGVE VPKLVQRLRE
     EFGDKVATRR TGWKLTWDVR RSKVVVEEAS GKKWEQKVGE LPPNVQEIIA RGGLEKWVKS
     QIEA