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 27-MAR-2024, entry version 95.
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; 237631.Q4P521; -.
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; 1122834at2759; -.
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; cd01582; Homoaconitase; 1.
DR CDD; cd01674; Homoaconitase_Swivel; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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 NCBIfam; TIGR00139; h_aconitase; 1.
DR PANTHER; PTHR43822:SF25; HOMOACONITASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 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
//
