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Protein

Aconitate hydratase, mitochondrial

Gene

ACO1

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

Functioni

Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle. Can also provide minor contributions to the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis. Plays also an essential role in mtDNA maintenance. May directly protect mtDNA from accumulation of point mutations and ssDNA breaks as a component of mitochondrial nucleoids, or by preventing accumulation of iron citrate thereby alleviating its detrimental effects in mitochondria.5 Publications

Catalytic activityi

Citrate = isocitrate.

Cofactori

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

Enzyme regulationi

Subject to catabolite regulation.

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 2 of the subpathway that synthesizes isocitrate from oxaloacetate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Citrate synthase 3, mitochondrial (CIT3), Citrate synthase, mitochondrial (CIT1), Citrate synthase, peroxisomal (CIT2)
  2. Aconitate hydratase, mitochondrial (ACO1)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isocitrate from oxaloacetate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951SubstrateBy similarity
Metal bindingi382 – 3821Iron-sulfur (4Fe-4S)By similarity
Metal bindingi445 – 4451Iron-sulfur (4Fe-4S)By similarity
Metal bindingi448 – 4481Iron-sulfur (4Fe-4S)By similarity
Binding sitei471 – 4711SubstrateBy similarity
Binding sitei476 – 4761SubstrateBy similarity
Binding sitei604 – 6041SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • mitochondrial genome maintenance Source: SGD
  • protein targeting to mitochondrion Source: Reactome
  • tricarboxylic acid cycle Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:YLR304C-MONOMER.
YEAST:YLR304C-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.
UniPathwayiUPA00223; UER00718.

Names & Taxonomyi

Protein namesi
Recommended name:
Aconitate hydratase, mitochondrial (EC:4.2.1.3)
Short name:
Aconitase
Alternative name(s):
Citrate hydro-lyase
Gene namesi
Name:ACO1
Synonyms:GLU1
Ordered Locus Names:YLR304C
ORF Names:L8003.22
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR304C.
SGDiS000004295. ACO1.

Subcellular locationi

  • Mitochondrion
  • Cytoplasm

  • Note: Mainly mitochondrial, small amounts are also detected in the cytosol with a ratio of 94:6.

GO - Cellular componenti

  • cytosol Source: SGD
  • mitochondrial intermembrane space Source: Reactome
  • mitochondrial matrix Source: SGD
  • mitochondrial nucleoid Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Essential for growth on nonfermentable carbon sources and for biosynthesis of glutamate. Causes a dramatic increase in cellular citrate levels.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi604 – 6041R → K: Strongly diminishes the catalytic activity towards both known substrates, aconitate and homoaconitate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1616Mitochondrion1 PublicationAdd
BLAST
Chaini17 – 778762Aconitate hydratase, mitochondrialPRO_0000000547Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei391 – 3911PhosphoserineCombined sources
Modified residuei409 – 4091PhosphothreonineCombined sources
Modified residuei556 – 5561PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP19414.
PRIDEiP19414.
TopDownProteomicsiP19414.

PTM databases

iPTMnetiP19414.

Expressioni

Inductioni

Highly induced in the absence of glutamate. Induction is further increased when both glutamate and lysine are missing.1 Publication

Interactioni

Subunit structurei

Monomer. Binds to mitochondrial DNA (mtDNA) and identified as component of mitochondrial nucleoids.2 Publications

Protein-protein interaction databases

BioGridi31569. 175 interactions.
DIPiDIP-4679N.
IntActiP19414. 10 interactions.
MINTiMINT-557728.

Structurei

3D structure databases

ProteinModelPortaliP19414.
SMRiP19414. Positions 26-778.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni188 – 1903Substrate bindingBy similarity
Regioni667 – 6682Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00840000129913.
HOGENOMiHOG000224293.
InParanoidiP19414.
KOiK01681.
OMAiCTELAPG.
OrthoDBiEOG092C0DQS.

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.

P19414-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSARSAIKR PIVRGLATVS NLTRDSKVNQ NLLEDHSFIN YKQNVETLDI
60 70 80 90 100
VRKRLNRPFT YAEKILYGHL DDPHGQDIQR GVSYLKLRPD RVACQDATAQ
110 120 130 140 150
MAILQFMSAG LPQVAKPVTV HCDHLIQAQV GGEKDLKRAI DLNKEVYDFL
160 170 180 190 200
ASATAKYNMG FWKPGSGIIH QIVLENYAFP GALIIGTDSH TPNAGGLGQL
210 220 230 240 250
AIGVGGADAV DVMAGRPWEL KAPKILGVKL TGKMNGWTSP KDIILKLAGI
260 270 280 290 300
TTVKGGTGKI VEYFGDGVDT FSATGMGTIC NMGAEIGATT SVFPFNKSMI
310 320 330 340 350
EYLEATGRGK IADFAKLYHK DLLSADKDAE YDEVVEIDLN TLEPYINGPF
360 370 380 390 400
TPDLATPVSK MKEVAVANNW PLDVRVGLIG SCTNSSYEDM SRSASIVKDA
410 420 430 440 450
AAHGLKSKTI FTVTPGSEQI RATIERDGQL ETFKEFGGIV LANACGPCIG
460 470 480 490 500
QWDRRDIKKG DKNTIVSSYN RNFTSRNDGN PQTHAFVASP ELVTAFAIAG
510 520 530 540 550
DLRFNPLTDK LKDKDGNEFM LKPPHGDGLP QRGYDAGENT YQAPPADRST
560 570 580 590 600
VEVKVSPTSD RLQLLKPFKP WDGKDAKDMP ILIKAVGKTT TDHISMAGPW
610 620 630 640 650
LKYRGHLENI SNNYMIGAIN AENKKANCVK NVYTGEYKGV PDTARDYRDQ
660 670 680 690 700
GIKWVVIGDE NFGEGSSREH AALEPRFLGG FAIITKSFAR IHETNLKKQG
710 720 730 740 750
LLPLNFKNPA DYDKINPDDR IDILGLAELA PGKPVTMRVH PKNGKPWDAV
760 770
LTHTFNDEQI EWFKYGSALN KIKADEKK
Length:778
Mass (Da):85,368
Last modified:November 1, 1995 - v2
Checksum:iAA9EB9A24388090E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti527 – 54923DGLPQ…PADRS → RWFASKEVMMLVRTLTKLHL QTVA in AAA34389 (PubMed:1972545).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33131 Genomic DNA. Translation: AAA34389.1.
U17243 Genomic DNA. Translation: AAB67348.1.
BK006945 Genomic DNA. Translation: DAA09613.1.
PIRiS50387.
RefSeqiNP_013407.1. NM_001182192.1.

Genome annotation databases

EnsemblFungiiYLR304C; YLR304C; YLR304C.
GeneIDi851013.
KEGGisce:YLR304C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33131 Genomic DNA. Translation: AAA34389.1.
U17243 Genomic DNA. Translation: AAB67348.1.
BK006945 Genomic DNA. Translation: DAA09613.1.
PIRiS50387.
RefSeqiNP_013407.1. NM_001182192.1.

3D structure databases

ProteinModelPortaliP19414.
SMRiP19414. Positions 26-778.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31569. 175 interactions.
DIPiDIP-4679N.
IntActiP19414. 10 interactions.
MINTiMINT-557728.

PTM databases

iPTMnetiP19414.

Proteomic databases

MaxQBiP19414.
PRIDEiP19414.
TopDownProteomicsiP19414.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR304C; YLR304C; YLR304C.
GeneIDi851013.
KEGGisce:YLR304C.

Organism-specific databases

EuPathDBiFungiDB:YLR304C.
SGDiS000004295. ACO1.

Phylogenomic databases

GeneTreeiENSGT00840000129913.
HOGENOMiHOG000224293.
InParanoidiP19414.
KOiK01681.
OMAiCTELAPG.
OrthoDBiEOG092C0DQS.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00718.
BioCyciMetaCyc:YLR304C-MONOMER.
YEAST:YLR304C-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Miscellaneous databases

PROiP19414.

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...

Entry informationi

Entry nameiACON_YEAST
AccessioniPrimary (citable) accession number: P19414
Secondary accession number(s): D6VYU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1995
Last modified: September 7, 2016
This is version 163 of the entry and version 2 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 96700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.