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Protein

Homoaconitase, mitochondrial

Gene

LYS4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi340 – 3401Iron-sulfur (4Fe-4S)By similarity
Metal bindingi407 – 4071Iron-sulfur (4Fe-4S)By similarity
Metal bindingi410 – 4101Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: InterPro
  2. homoaconitate hydratase activity Source: SGD
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. lysine biosynthetic process via aminoadipic acid Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Lysine biosynthesis

Keywords - Ligandi

Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YDR234W-MONOMER.
UniPathwayiUPA00033; UER01027.

Names & Taxonomyi

Protein namesi
Recommended name:
Homoaconitase, mitochondrial (EC:4.2.1.36)
Alternative name(s):
Homoaconitate hydratase
Gene namesi
Name:LYS4
Synonyms:LYS3
Ordered Locus Names:YDR234W
ORF Names:YD8419.01, YD9934.18
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR234w.
SGDiS000002642. LYS4.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2020MitochondrionSequence AnalysisAdd
BLAST
Chaini21 – 693673Homoaconitase, mitochondrialPRO_0000000551Add
BLAST

Proteomic databases

MaxQBiP49367.
PaxDbiP49367.
PeptideAtlasiP49367.

Expressioni

Gene expression databases

GenevestigatoriP49367.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
RSP5P399402EBI-10276,EBI-16219

Protein-protein interaction databases

BioGridi32285. 25 interactions.
IntActiP49367. 1 interaction.
MINTiMINT-2732625.
STRINGi4932.YDR234W.

Structurei

3D structure databases

ProteinModelPortaliP49367.
SMRiP49367. Positions 20-693.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1048.
GeneTreeiENSGT00730000114222.
HOGENOMiHOG000173778.
InParanoidiP49367.
KOiK01705.
OMAiSWPVATK.
OrthoDBiEOG70CRGK.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProiIPR015931. 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]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF8. PTHR11670:SF8. 1 hit.
PfamiPF00330. Aconitase. 2 hits.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR00139. h_aconitase. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49367-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLRSTTFTRS FHSSRAWLKG QNLTEKIVQS YAVNLPEGKV VHSGDYVSIK
60 70 80 90 100
PAHCMSHDNS WPVALKFMGL GATKIKNPSQ IVTTLDHDIQ NKSEKNLTKY
110 120 130 140 150
KNIENFAKKH HIDHYPAGRG IGHQIMIEEG YAFPLNMTVA SDSHSNTYGG
160 170 180 190 200
LGSLGTPIVR TDAAAIWATG QTWWQIPPVA QVELKGQLPQ GVSGKDIIVA
210 220 230 240 250
LCGLFNNDQV LNHAIEFTGD SLNALPIDHR LTIANMTTEW GALSGLFPVD
260 270 280 290 300
KTLIDWYKNR LQKLGTNNHP RINPKTIRAL EEKAKIPKAD KDAHYAKKLI
310 320 330 340 350
IDLATLTHYV SGPNSVKVSN TVQDLSQQDI KINKAYLVSC TNSRLSDLQS
360 370 380 390 400
AADVVCPTGD LNKVNKVAPG VEFYVAAASS EIEADARKSG AWEKLLKAGC
410 420 430 440 450
IPLPSGCGPC IGLGAGLLEP GEVGISATNR NFKGRMGSKD ALAYLASPAV
460 470 480 490 500
VAASAVLGKI SSPAEVLSTS EIPFSGVKTE IIENPVVEEE VNAQTEAPKQ
510 520 530 540 550
SVEILEGFPR EFSGELVLCD ADNINTDGIY PGKYTYQDDV PKEKMAQVCM
560 570 580 590 600
ENYDAEFRTK VHPGDIVVSG FNFGTGSSRE QAATALLAKG INLVVSGSFG
610 620 630 640 650
NIFSRNSINN ALLTLEIPAL IKKLREKYQG APKELTRRTG WFLKWDVADA
660 670 680 690
KVVVTEGSLD GPVILEQKVG ELGKNLQEII VKGGLEGWVK SQL
Length:693
Mass (Da):75,151
Last modified:February 1, 1996 - v1
Checksum:i9342E3CF83FE3FD2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti581 – 5811Q → R in AAU09698. (PubMed:17322287)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS61067.
RefSeqiNP_010520.3. NM_001180542.3.

Genome annotation databases

EnsemblFungiiYDR234W; YDR234W; YDR234W.
GeneIDi851820.
KEGGisce:YDR234W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS61067.
RefSeqiNP_010520.3. NM_001180542.3.

3D structure databases

ProteinModelPortaliP49367.
SMRiP49367. Positions 20-693.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32285. 25 interactions.
IntActiP49367. 1 interaction.
MINTiMINT-2732625.
STRINGi4932.YDR234W.

Proteomic databases

MaxQBiP49367.
PaxDbiP49367.
PeptideAtlasiP49367.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR234W; YDR234W; YDR234W.
GeneIDi851820.
KEGGisce:YDR234W.

Organism-specific databases

CYGDiYDR234w.
SGDiS000002642. LYS4.

Phylogenomic databases

eggNOGiCOG1048.
GeneTreeiENSGT00730000114222.
HOGENOMiHOG000173778.
InParanoidiP49367.
KOiK01705.
OMAiSWPVATK.
OrthoDBiEOG70CRGK.

Enzyme and pathway databases

UniPathwayiUPA00033; UER01027.
BioCyciYEAST:YDR234W-MONOMER.

Miscellaneous databases

NextBioi969689.

Gene expression databases

GenevestigatoriP49367.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProiIPR015931. 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]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF8. PTHR11670:SF8. 1 hit.
PfamiPF00330. Aconitase. 2 hits.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR00139. h_aconitase. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. 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.

Entry informationi

Entry nameiLYS4_YEAST
AccessioniPrimary (citable) accession number: P49367
Secondary accession number(s): D6VSL5, Q66RF2, Q7LH77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 7, 2015
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7350 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.