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Protein

Homocitrate dehydratase, mitochondrial

Gene

ACO2

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 dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.1 Publication

Catalytic activityi

(R)-2-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: L-lysine biosynthesis via AAA pathway

This protein is involved in step 2 of the subpathway that synthesizes L-alpha-aminoadipate from 2-oxoglutarate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Homocitrate synthase, cytosolic isozyme (LYS20), Homocitrate synthase, mitochondrial (LYS21)
  2. Homocitrate dehydratase, mitochondrial (ACO2)
  3. Homoaconitase, mitochondrial (LYS4)
  4. Homoisocitrate dehydrogenase, mitochondrial (LYS12)
  5. Aromatic/aminoadipate aminotransferase 1 (ARO8)
This subpathway is part of the pathway L-lysine biosynthesis via AAA pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-alpha-aminoadipate from 2-oxoglutarate, the pathway L-lysine biosynthesis via AAA pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei96 – 961SubstrateBy similarity
Metal bindingi385 – 3851Iron-sulfur (4Fe-4S)By similarity
Metal bindingi448 – 4481Iron-sulfur (4Fe-4S)By similarity
Metal bindingi451 – 4511Iron-sulfur (4Fe-4S)By similarity
Binding sitei476 – 4761SubstrateBy similarity
Binding sitei481 – 4811SubstrateBy similarity

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • aconitate hydratase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Lysine biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YJL200C-MONOMER.
ReactomeiR-SCE-71403. Citric acid cycle (TCA cycle).
UniPathwayiUPA00033; UER00029.

Names & Taxonomyi

Protein namesi
Recommended name:
Homocitrate dehydratase, mitochondrial (EC:4.2.1.-)
Alternative name(s):
Aconitase 2
Gene namesi
Name:ACO2
Ordered Locus Names:YJL200C
ORF Names:J0327
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL200C.
SGDiS000003736. ACO2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Has very little effect on growth on nonfermentable carbon sources.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi610 – 6101K → R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1414MitochondrionSequence analysisAdd
BLAST
Chaini15 – 789775Homocitrate dehydratase, mitochondrialPRO_0000076649Add
BLAST

Proteomic databases

MaxQBiP39533.

PTM databases

iPTMnetiP39533.

Expressioni

Inductioni

Constitutively expressed with a small induction when both glutamate and lysine are missing.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi33557. 64 interactions.
DIPiDIP-1376N.
IntActiP39533. 8 interactions.
MINTiMINT-403220.

Structurei

3D structure databases

ProteinModelPortaliP39533.
SMRiP39533. Positions 35-787.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni189 – 1913Substrate bindingBy similarity
Regioni672 – 6732Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00840000129865.
HOGENOMiHOG000224293.
InParanoidiP39533.
KOiK17450.
OMAiGDAQFNP.
OrthoDBiEOG7X6M7Q.

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.
IPR006248. Aconitase_mito-like.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR01340. aconitase_mito. 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.

P39533-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSSANRFYI KRHLATHANM FPSVSKNFQT KVPPYAKLLT NLDKIKQITN
60 70 80 90 100
NAPLTLAEKI LYSHLCDPEE SITSSDLSTI RGNKYLKLNP DRVAMQDASA
110 120 130 140 150
QMALLQFMTT GLNQTSVPAS IHCDHLIVGK DGETKDLPSS IATNQEVFDF
160 170 180 190 200
LESCAKRYGI QFWGPGSGII HQIVLENFSA PGLMMLGTDS HTPNAGGLGA
210 220 230 240 250
IAIGVGGADA VDALTGTPWE LKAPKILGVK LTGKLNGWST PKDVITKLAG
260 270 280 290 300
LLTVRGGTGY IVEYFGEGVS TLSCTGMATI CNMGAEIGAT TSTFPYQEAH
310 320 330 340 350
KRYLQATNRA EVAEAADVAL NKFNFLRADK DAQYDKVIEI DLSAIEPHVN
360 370 380 390 400
GPFTPDLSTP ISQYAEKSLK ENWPQKVSAG LIGSCTNSSY QDMSRVVDLV
410 420 430 440 450
KQASKAGLKP RIPFFVTPGS EQIRATLERD GIIDIFQENG AKVLANACGP
460 470 480 490 500
CIGQWNREDV SKTSKETNTI FTSFNRNFRA RNDGNRNTMN FLTSPEIVTA
510 520 530 540 550
MSYSGDAQFN PLTDSIKLPN GKDFKFQPPK GDELPKRGFE HGRDKFYPEM
560 570 580 590 600
DPKPDSNVEI KVDPNSDRLQ LLEPFKPWNG KELKTNVLLK VEGKCTTDHI
610 620 630 640 650
SAAGVWLKYK GHLENISYNT LIGAQNKETG EVNKAYDLDG TEYDIPGLMM
660 670 680 690 700
KWKSDGRPWT VIAEHNYGEG SAREHAALSP RFLGGEILLV KSFARIHETN
710 720 730 740 750
LKKQGVLPLT FANESDYDKI SSGDVLETLN LVDMIAKDGN NGGEIDVKIT
760 770 780
KPNGESFTIK AKHTMSKDQI DFFKAGSAIN YIGNIRRNE
Length:789
Mass (Da):86,583
Last modified:February 1, 1995 - v1
Checksum:iFABA4FE482D3F993
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77688 Genomic DNA. Translation: CAA54757.1.
Z49475 Genomic DNA. Translation: CAA89495.1.
BK006943 Genomic DNA. Translation: DAA08609.1.
PIRiS46631.
RefSeqiNP_012335.1. NM_001181633.1.

Genome annotation databases

EnsemblFungiiYJL200C; YJL200C; YJL200C.
GeneIDi853230.
KEGGisce:YJL200C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77688 Genomic DNA. Translation: CAA54757.1.
Z49475 Genomic DNA. Translation: CAA89495.1.
BK006943 Genomic DNA. Translation: DAA08609.1.
PIRiS46631.
RefSeqiNP_012335.1. NM_001181633.1.

3D structure databases

ProteinModelPortaliP39533.
SMRiP39533. Positions 35-787.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33557. 64 interactions.
DIPiDIP-1376N.
IntActiP39533. 8 interactions.
MINTiMINT-403220.

PTM databases

iPTMnetiP39533.

Proteomic databases

MaxQBiP39533.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL200C; YJL200C; YJL200C.
GeneIDi853230.
KEGGisce:YJL200C.

Organism-specific databases

EuPathDBiFungiDB:YJL200C.
SGDiS000003736. ACO2.

Phylogenomic databases

GeneTreeiENSGT00840000129865.
HOGENOMiHOG000224293.
InParanoidiP39533.
KOiK17450.
OMAiGDAQFNP.
OrthoDBiEOG7X6M7Q.

Enzyme and pathway databases

UniPathwayiUPA00033; UER00029.
BioCyciYEAST:YJL200C-MONOMER.
ReactomeiR-SCE-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

PROiP39533.

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.
IPR006248. Aconitase_mito-like.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR01340. aconitase_mito. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of a 36 kb segment on the left arm of yeast chromosome X identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6, CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two homologues to chromosome III genes."
    Purnelle B., Coster F., Goffeau A.
    Yeast 10:1235-1249(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Genetic and biochemical interactions involving tricarboxylic acid cycle (TCA) function using a collection of mutants defective in all TCA cycle genes."
    Przybyla-Zawislak B., Gadde D.M., Ducharme K., McCammon M.T.
    Genetics 152:153-166(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. "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, INDUCTION, MUTAGENESIS OF LYS-610.

Entry informationi

Entry nameiACON2_YEAST
AccessioniPrimary (citable) accession number: P39533
Secondary accession number(s): D6VVZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The fermenting yeast S.cerevisiae has 2 aconitases, ACO1 essential for the citric acid cycle, and ACO2 specifically and exclusively contributing to lysine biosynthesis. In contrast, in respiring filamentous fungi the ACO2 homologs (acoB) seem enzymatically inactive and the ACO1 homolog (acoA) is solely responsible for these functions.
Present with 4670 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

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 one 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.