LYS4_YEAST
ID LYS4_YEAST Reviewed; 693 AA.
AC P49367; D6VSL5; Q66RF2; Q7LH77;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Homoaconitase, mitochondrial;
DE EC=4.2.1.36;
DE AltName: Full=Homoaconitate hydratase;
DE Flags: Precursor;
GN Name=LYS4; Synonyms=LYS3; OrderedLocusNames=YDR234W;
GN ORFNames=YD8419.01, YD9934.18;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9541534; DOI=10.1007/pl00006319;
RA Irvin S.D., Bhattacharjee J.K.;
RT "A unique fungal lysine biosynthesis enzyme shares a common ancestor with
RT tricarboxylic acid cycle and leucine biosynthetic enzymes found in diverse
RT organisms.";
RL J. Mol. Evol. 46:401-408(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RA Gamonet F., Lauquin G.J.-M.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION.
RX PubMed=2507177; DOI=10.1007/bf00411077;
RA Wang L., Okamoto S., Bhattacharjee J.K.;
RT "Cloning and physical characterization of linked lysine genes (lys4, lys15)
RT of Saccharomyces cerevisiae.";
RL Curr. Genet. 16:7-12(1989).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP FUNCTION.
RX PubMed=23106124; DOI=10.1111/mmi.12076;
RA Fazius F., Shelest E., Gebhardt P., Brock M.;
RT "The fungal alpha-aminoadipate pathway for lysine biosynthesis requires two
RT enzymes of the aconitase family for the isomerization of homocitrate to
RT homoisocitrate.";
RL Mol. Microbiol. 86:1508-1530(2012).
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:23106124,
CC ECO:0000269|PubMed:2507177}.
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 -!- INTERACTION:
CC P49367; P39940: RSP5; NbExp=2; IntAct=EBI-10276, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; U46154; AAA88902.1; -; Genomic_DNA.
DR EMBL; X93502; CAA63764.1; -; Genomic_DNA.
DR EMBL; Z48612; CAA88513.1; -; Genomic_DNA.
DR EMBL; Z49701; CAA89720.1; -; Genomic_DNA.
DR EMBL; AY723781; AAU09698.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12075.1; -; Genomic_DNA.
DR PIR; S61067; S61067.
DR RefSeq; NP_010520.3; NM_001180542.3.
DR AlphaFoldDB; P49367; -.
DR SMR; P49367; -.
DR BioGRID; 32285; 50.
DR IntAct; P49367; 1.
DR MINT; P49367; -.
DR STRING; 4932.YDR234W; -.
DR MaxQB; P49367; -.
DR PaxDb; P49367; -.
DR PRIDE; P49367; -.
DR EnsemblFungi; YDR234W_mRNA; YDR234W; YDR234W.
DR GeneID; 851820; -.
DR KEGG; sce:YDR234W; -.
DR SGD; S000002642; LYS4.
DR VEuPathDB; FungiDB:YDR234W; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_3_1_1; -.
DR InParanoid; P49367; -.
DR OMA; VMIRPEH; -.
DR BioCyc; YEAST:YDR234W-MON; -.
DR BRENDA; 4.2.1.36; 984.
DR UniPathway; UPA00033; UER01027.
DR PRO; PR:P49367; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P49367; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0004409; F:homoaconitate hydratase activity; ISA: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..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..693
FT /note="Homoaconitase, mitochondrial"
FT /id="PRO_0000000551"
FT BINDING 340
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT CONFLICT 581
FT /note="Q -> R (in Ref. 5; AAU09698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 693 AA; 75151 MW; 9342E3CF83FE3FD2 CRC64;
MLRSTTFTRS FHSSRAWLKG QNLTEKIVQS YAVNLPEGKV VHSGDYVSIK PAHCMSHDNS
WPVALKFMGL GATKIKNPSQ IVTTLDHDIQ NKSEKNLTKY KNIENFAKKH HIDHYPAGRG
IGHQIMIEEG YAFPLNMTVA SDSHSNTYGG LGSLGTPIVR TDAAAIWATG QTWWQIPPVA
QVELKGQLPQ GVSGKDIIVA LCGLFNNDQV LNHAIEFTGD SLNALPIDHR LTIANMTTEW
GALSGLFPVD KTLIDWYKNR LQKLGTNNHP RINPKTIRAL EEKAKIPKAD KDAHYAKKLI
IDLATLTHYV SGPNSVKVSN TVQDLSQQDI KINKAYLVSC TNSRLSDLQS AADVVCPTGD
LNKVNKVAPG VEFYVAAASS EIEADARKSG AWEKLLKAGC IPLPSGCGPC IGLGAGLLEP
GEVGISATNR NFKGRMGSKD ALAYLASPAV VAASAVLGKI SSPAEVLSTS EIPFSGVKTE
IIENPVVEEE VNAQTEAPKQ SVEILEGFPR EFSGELVLCD ADNINTDGIY PGKYTYQDDV
PKEKMAQVCM ENYDAEFRTK VHPGDIVVSG FNFGTGSSRE QAATALLAKG INLVVSGSFG
NIFSRNSINN ALLTLEIPAL IKKLREKYQG APKELTRRTG WFLKWDVADA KVVVTEGSLD
GPVILEQKVG ELGKNLQEII VKGGLEGWVK SQL
