ID   LYS4_EMENI              Reviewed;         776 AA.
AC   Q92412; C8V0K3; Q5AYV9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Homoaconitase, mitochondrial;
DE            EC=4.2.1.36 {ECO:0000269|PubMed:9268014};
DE   AltName: Full=Homoaconitate hydratase;
DE   Flags: Precursor;
GN   Name=lys4; Synonyms=lysF; ORFNames=AN6521;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9268014; DOI=10.1007/s004380050494;
RA   Weidner G., Steffan B., Brakhage A.A.;
RT   "The Aspergillus nidulans lysF gene encodes homoaconitase, an enzyme
RT   involved in the fungus-specific lysine biosynthesis pathway.";
RL   Mol. Gen. Genet. 255:237-247(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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:0000269|PubMed:9268014}.
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:0000269|PubMed:9268014};
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.1 mM for homoisocitric acid {ECO:0000269|PubMed:9268014};
CC       pH dependence:
CC         Optimum pH is 8.1-8.6. {ECO:0000269|PubMed:9268014};
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; X99624; CAA67943.1; -; Genomic_DNA.
DR   EMBL; AACD01000109; EAA57861.1; -; Genomic_DNA.
DR   EMBL; BN001301; CBF70908.1; -; Genomic_DNA.
DR   RefSeq; XP_664125.1; XM_659033.1.
DR   AlphaFoldDB; Q92412; -.
DR   SMR; Q92412; -.
DR   STRING; 162425.CADANIAP00007293; -.
DR   EnsemblFungi; CBF70908; CBF70908; ANIA_06521.
DR   EnsemblFungi; EAA57861; EAA57861; AN6521.2.
DR   GeneID; 2870212; -.
DR   KEGG; ani:AN6521.2; -.
DR   eggNOG; KOG0453; Eukaryota.
DR   HOGENOM; CLU_006714_3_1_1; -.
DR   InParanoid; Q92412; -.
DR   OMA; LTYQDNV; -.
DR   OrthoDB; 265826at2759; -.
DR   BRENDA; 4.2.1.36; 517.
DR   UniPathway; UPA00033; UER01027.
DR   Proteomes; UP000000560; Chromosome I.
DR   Proteomes; UP000005890; 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; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IMP:SGD.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Iron; Iron-sulfur; Lyase; Lysine biosynthesis;
KW   Metal-binding; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..38
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..776
FT                   /note="Homoaconitase, mitochondrial"
FT                   /id="PRO_0000000550"
FT   BINDING         394
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         463
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         466
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        424..425
FT                   /note="AD -> H (in Ref. 1; CAA67943)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   776 AA;  84087 MW;  349ECFEB965420F1 CRC64;
     MQSRLVSQSG LGRRWAVLRC ALSKTYQRRT LTSTRRQFQD VFQSQLEDPT SAALFSALNS
     SKAVPQTLTE KIVQKYSVGL PQGKFVKSGD YVTIQPHRCM THDNSWPCAL KFMSIGASRL
     HNPDQIVMTL DHDVQNKSDK NLKKYRQIEE FATQHGVEFY PAGRGIGHQI MIEEGFAWPG
     TLAVASDSHS NMYGGVGCLG TPIVRTDAAS VWATGKTWWQ IPPVAKVTFK GVLPPGVTGK
     DVIVALCGLF NKDDVLNHAI EFTGSEETMR SLSVDTRLTI ANMTTEWGAL SGLFPIDSVL
     KGWLRGKATT AAMGLADGPF KTRAAERFTH PLLEQLFENP LTADKGAKYA KELFLDLSSL
     SPYVSGPNSV KVATPLKELE AQNIKVDKAY LVSCTNSRAS DIAAAAKVFK EAAEKNGGKI
     PKIADGVKFY IAAASIPEQL AAEGNGDWQT LLEAGATQLP AGCGPCIGMG QGLLEPGEVG
     ISASNRNFKG RMGSTEAKAY LGSPEVVAAS ALSGKLSGPG WYQTPEGWTE VIRGEGDGIR
     EEDRMLTNEE ALEKIIGQLD DLVADGEKRF ASETPAVEES EQGLTEIYPG FPERVSGELV
     FCDADNVNTD GIYPGKYTYQ DDVPPETMAR VCMENYDPEF STTAKEGDIL VSGFNFGCGS
     SREQAATAIL AKKIPLVVSG SFGNIFSRNS INNALMGLEV PRLVNRLRET FGSGDKVLTR
     RTGWTLTWDV RKSQIEVQEG PGGPKWTHKV GELPPNVQEI IAKGGLEKWV KNAIGA