ID   LYS4_USTMA              Reviewed;         734 AA.
AC   Q4P521; A0A0D1CID6;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Homoaconitase, mitochondrial;
DE            EC=4.2.1.36;
DE   AltName: Full=Homoaconitate hydratase;
DE   Flags: Precursor;
GN   Name=LYS4; ORFNames=UMAG_10689;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-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: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; CM003156; KIS66728.1; -; Genomic_DNA.
DR   RefSeq; XP_011391741.1; XM_011393439.1.
DR   AlphaFoldDB; Q4P521; -.
DR   SMR; Q4P521; -.
DR   STRING; 5270.UM04792P0; -.
DR   EnsemblFungi; KIS66728; KIS66728; UMAG_10689.
DR   GeneID; 23566684; -.
DR   KEGG; uma:UMAG_10689; -.
DR   VEuPathDB; FungiDB:UMAG_10689; -.
DR   eggNOG; KOG0453; Eukaryota.
DR   HOGENOM; CLU_006714_3_1_1; -.
DR   InParanoid; Q4P521; -.
DR   OrthoDB; 265826at2759; -.
DR   UniPathway; UPA00033; UER01027.
DR   Proteomes; UP000000561; Chromosome 17.
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; 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..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..734
FT                   /note="Homoaconitase, mitochondrial"
FT                   /id="PRO_0000247928"
FT   BINDING         367
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         427
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         430
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   734 AA;  77591 MW;  F92E67B266DFD9E7 CRC64;
     MGASNLLRFG AVTRISTPLL SRRSLATHAA VNPASGTYNL VEKIVQKYAV DLSPGSHVKS
     GDYVSIRPGT VMTHDNTGPV ISKFGSIGAT SIYNPDQVVF ALDHDVQNKS AKNLEKYSKI
     ESFARKHGID FYPAGRGIGH QVLVEEGYAF PQTLAVASDS HSNMYGGVGC LGTPIVRTDA
     AAIWATGQTW WQIPEVVKVE LKGELPKGVT GKDVIVALCG YFNKDQVLNA AIEFHGSGLS
     SLSVEERLAI ANMTTEWGAL AGLFPTDDVT LSWYEKQIRK RDKLEFQIGS SPSPSNSHPR
     LNMNRLDELS RTLLRPDSGA VYSKHLTLDL ATLVPHVSGP NSVKVSTPLD ELTSQNIAIN
     KAYLVSCVNS RASDLKAAAD VIRGKKVAPG VEFYVAAASS VVQREAEEAG DWGALMAAGA
     KPLPAGCGPC IGLGVGLLED GEVGISATNR NYKGRMGSPN AQAYLASPAV VAASAIEGKI
     CGPSDLDVSL LPPSKGLKYS ISTAANAAPA DASSTDASAG GVEILDSFPT AFSGPLIFAP
     QDNLNTDGIY PGKYTYQDDI TPEKQAEVVM ENYDASFAST VAGLRASSSS SSSTKQGPIL
     IGGYNFGTGS SREQAATALK YAGIPLVLAG SFGDIFQRNA INNGLICLES HQLVQDLTRL
     YLENEGGVRN SKAILLDESK VHIDSSTGSI NLSFKGPDGA KIERTYTAKP AGIGRSVQEI
     YTAGGLEKWV KQRI