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P49367 (LYS4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Homoaconitase, mitochondrial

EC=4.2.1.36
Alternative name(s):
Homoaconitate hydratase
Gene names
Name:LYS4
Synonyms:LYS3
Ordered Locus Names:YDR234W
ORF Names:YD8419.01, YD9934.18
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible hydration of cis-homoaconitate to (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for lysine biosynthesis. Ref.6 Ref.9

Catalytic activity

(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate = (Z)-but-1-ene-1,2,4-tricarboxylate + H2O.

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 3/5.

Subcellular location

Mitochondrion Ref.7.

Miscellaneous

Present with 7350 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RSP5P399402EBI-10276,EBI-16219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2020Mitochondrion Potential
Chain21 – 693673Homoaconitase, mitochondrial
PRO_0000000551

Sites

Metal binding3401Iron-sulfur (4Fe-4S) By similarity
Metal binding4071Iron-sulfur (4Fe-4S) By similarity
Metal binding4101Iron-sulfur (4Fe-4S) By similarity

Experimental info

Sequence conflict5811Q → R in AAU09698. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P49367 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9342E3CF83FE3FD2

FASTA69375,151
        10         20         30         40         50         60 
MLRSTTFTRS FHSSRAWLKG QNLTEKIVQS YAVNLPEGKV VHSGDYVSIK PAHCMSHDNS 

        70         80         90        100        110        120 
WPVALKFMGL GATKIKNPSQ IVTTLDHDIQ NKSEKNLTKY KNIENFAKKH HIDHYPAGRG 

       130        140        150        160        170        180 
IGHQIMIEEG YAFPLNMTVA SDSHSNTYGG LGSLGTPIVR TDAAAIWATG QTWWQIPPVA 

       190        200        210        220        230        240 
QVELKGQLPQ GVSGKDIIVA LCGLFNNDQV LNHAIEFTGD SLNALPIDHR LTIANMTTEW 

       250        260        270        280        290        300 
GALSGLFPVD KTLIDWYKNR LQKLGTNNHP RINPKTIRAL EEKAKIPKAD KDAHYAKKLI 

       310        320        330        340        350        360 
IDLATLTHYV SGPNSVKVSN TVQDLSQQDI KINKAYLVSC TNSRLSDLQS AADVVCPTGD 

       370        380        390        400        410        420 
LNKVNKVAPG VEFYVAAASS EIEADARKSG AWEKLLKAGC IPLPSGCGPC IGLGAGLLEP 

       430        440        450        460        470        480 
GEVGISATNR NFKGRMGSKD ALAYLASPAV VAASAVLGKI SSPAEVLSTS EIPFSGVKTE 

       490        500        510        520        530        540 
IIENPVVEEE VNAQTEAPKQ SVEILEGFPR EFSGELVLCD ADNINTDGIY PGKYTYQDDV 

       550        560        570        580        590        600 
PKEKMAQVCM ENYDAEFRTK VHPGDIVVSG FNFGTGSSRE QAATALLAKG INLVVSGSFG 

       610        620        630        640        650        660 
NIFSRNSINN ALLTLEIPAL IKKLREKYQG APKELTRRTG WFLKWDVADA KVVVTEGSLD 

       670        680        690 
GPVILEQKVG ELGKNLQEII VKGGLEGWVK SQL 

« Hide

References

« Hide 'large scale' references
[1]"A unique fungal lysine biosynthesis enzyme shares a common ancestor with tricarboxylic acid cycle and leucine biosynthetic enzymes found in diverse organisms."
Irvin S.D., Bhattacharjee J.K.
J. Mol. Evol. 46:401-408(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Gamonet F., Lauquin G.J.-M.
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S288c / GRF88.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"Cloning and physical characterization of linked lysine genes (lys4, lys15) of Saccharomyces cerevisiae."
Wang L., Okamoto S., Bhattacharjee J.K.
Curr. Genet. 16:7-12(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"The fungal alpha-aminoadipate pathway for lysine biosynthesis requires two enzymes of the aconitase family for the isomerization of homocitrate to homoisocitrate."
Fazius F., Shelest E., Gebhardt P., Brock M.
Mol. Microbiol. 86:1508-1530(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U46154 Genomic DNA. Translation: AAA88902.1.
X93502 Genomic DNA. Translation: CAA63764.1.
Z48612 Genomic DNA. Translation: CAA88513.1.
Z49701 Genomic DNA. Translation: CAA89720.1.
AY723781 Genomic DNA. Translation: AAU09698.1.
BK006938 Genomic DNA. Translation: DAA12075.1.
PIRS61067.
RefSeqNP_010520.3. NM_001180542.3.

3D structure databases

ProteinModelPortalP49367.
SMRP49367. Positions 23-693.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32285. 25 interactions.
IntActP49367. 1 interaction.
MINTMINT-2732625.
STRING4932.YDR234W.

Proteomic databases

MaxQBP49367.
PaxDbP49367.
PeptideAtlasP49367.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR234W; YDR234W; YDR234W.
GeneID851820.
KEGGsce:YDR234W.

Organism-specific databases

CYGDYDR234w.
SGDS000002642. LYS4.

Phylogenomic databases

eggNOGCOG1048.
GeneTreeENSGT00730000114222.
HOGENOMHOG000173778.
KOK01705.
OMASWPVATK.
OrthoDBEOG70CRGK.

Enzyme and pathway databases

BioCycYEAST:YDR234W-MONOMER.
UniPathwayUPA00033; UER01027.

Gene expression databases

GenevestigatorP49367.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
IPR004418. Homoaconitase_mito.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF8. PTHR11670:SF8. 1 hit.
PfamPF00330. Aconitase. 2 hits.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsTIGR00139. h_aconitase. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969689.

Entry information

Entry nameLYS4_YEAST
AccessionPrimary (citable) accession number: P49367
Secondary accession number(s): D6VSL5, Q66RF2, Q7LH77
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways