LYS4_CANGA
ID LYS4_CANGA Reviewed; 689 AA.
AC Q6FM51;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Homoaconitase, mitochondrial;
DE EC=4.2.1.36;
DE AltName: Full=Homoaconitate hydratase;
DE Flags: Precursor;
GN Name=LYS4; OrderedLocusNames=CAGL0K10978g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380957; CAG61656.1; -; Genomic_DNA.
DR RefSeq; XP_448693.1; XM_448693.1.
DR AlphaFoldDB; Q6FM51; -.
DR SMR; Q6FM51; -.
DR STRING; 5478.XP_448693.1; -.
DR EnsemblFungi; CAG61656; CAG61656; CAGL0K10978g.
DR GeneID; 2890081; -.
DR KEGG; cgr:CAGL0K10978g; -.
DR CGD; CAL0134839; CAGL0K10978g.
DR VEuPathDB; FungiDB:CAGL0K10978g; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_3_1_1; -.
DR InParanoid; Q6FM51; -.
DR UniPathway; UPA00033; UER01027.
DR Proteomes; UP000002428; Chromosome K.
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..689
FT /note="Homoaconitase, mitochondrial"
FT /id="PRO_0000000549"
FT BINDING 336
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 689 AA; 74540 MW; D69557A9FD81BF1D CRC64;
MVVLRRSFHV YTRLQRGQNL TEKIVQQYSV GLAPGKRVHS GDYVSIKPAH VMSHDNSWPV
ALKFMNLGAR TVKDPRQIVN TLDHDIQNKS DKNLTKYRNI ESFAKKHGID FYPAGRGIGH
QIMVEEGYAF PLNLTVASDS HSNTYGGMGA LGTPVVRTDA AAIWATGQTW WQIPPVAQVE
FKGKLHESVS GKDIIVALCG VFNKDQVLNH AIEFTGDAIK HLPVDFRLTI ANMTTEWGAL
SGLFPVDDTL INWYKNRLNI VGPNHPRINE TTIKNLEDKA KVFKADSDAV YAKKLVIDLS
TLTHYVSGPN SVKVSNTVQD LARDNIKINK AYLVSCTNAR LSDLESAAKV VCPTGDLSKV
NKVADGVEFY FAAASSEIEK EAAEKGIWQA LLAAGCKPLP SGCGPCIGLG AGLLEPGEVG
ISATNRNFKG RMGSKDALAY LASPAVVAAS AVLGRIGSPA EVWGIEDVKS SGLLAEELAC
NTETSTATPV SEGSAAKVEM LEGFPEEIVG ELVLCDADNV NTDGIYPGKY TYQDDVSRET
MAQVCMENYD GEFGSKANAG DILVSGFNFG TGSSREQAAT SLLAKGINLV VAGSFSNTFS
RNSINNALLT LEIPTLVEKL RSKFENAPKE LTRRTGWFLK WDVPNAKVYV TEGSPDGQVL
LEQKVGELGK NLQEIIIKGG LEGWVKSQL
