LYS4_KLULA
ID LYS4_KLULA Reviewed; 693 AA.
AC Q6CT61;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Homoaconitase, mitochondrial;
DE EC=4.2.1.36;
DE AltName: Full=Homoaconitate hydratase;
DE Flags: Precursor;
GN Name=LYS4; OrderedLocusNames=KLLA0C15125g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382123; CAH01729.1; -; Genomic_DNA.
DR RefSeq; XP_452878.1; XM_452878.1.
DR AlphaFoldDB; Q6CT61; -.
DR SMR; Q6CT61; -.
DR STRING; 28985.XP_452878.1; -.
DR EnsemblFungi; CAH01729; CAH01729; KLLA0_C15125g.
DR GeneID; 2891978; -.
DR KEGG; kla:KLLA0_C15125g; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_3_1_1; -.
DR InParanoid; Q6CT61; -.
DR OMA; VMIRPEH; -.
DR UniPathway; UPA00033; UER01027.
DR Proteomes; UP000000598; Chromosome C.
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..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..693
FT /note="Homoaconitase, mitochondrial"
FT /id="PRO_0000247925"
FT BINDING 338
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 693 AA; 74595 MW; FD4413B585D4DA7B CRC64;
MFRVQRLRMF STSRALYAGQ NMTEKIVQRH AVGLPEGKTV VSGDYVSIKP AHCMSHDNSW
PVALKFMGLG ASTIKNPRQV VNTLDHDVQN KSEKNLTKYK NIENFAKKHG IDFYPAGRGI
GHQIMIEEGY AFPLTMTVAS DSHSNTYGGI GALGTPIVRT DAAAIWATGQ TWWQIPPVAQ
VELKGELPAG ISGKDIIVAL CGVFNQDQVL NHAIEFTGDS LDKIPIDYRL TIANMTTEWG
ALSGLFPVDN VLLDFYRNRL TKVGNNHPRI NEARINELQA KSDSLQADPD AKYAKKLIID
LSTLTHYVSG PNSVKISSTV DDLSKQDIKV NKAYLVSCTN SRLSDLESAA NVVCPSGDIN
QVHKVAEGVE FYIAAASSEV EAEARATGAW QKLLNAGCLP LPAGCGPCIG LGTGLLEEGQ
VGISATNRNF KGRMGSKDAL AYLASPSVVA ASAILGKIGS PAEVLGTKDP NFTGVVATVE
DAPATSADGK DVADESGASG SVEILEGFPS EISGELVLCD ADNINTDGIY PGKYTYQDDV
PKETMAKVCM ENYDPDFQTK ANPGDILISG FNFGTGSSRE QAATAILAKG IKLVVSGSFG
NIFFRNSINN ALLTLEIPAL INMLRDRYKD APKELTRRTG WFLKWDVSQA KVYVTEGSVN
GPIVLEQKVG ELGKNLQEII VKGGLESWVK SQL
