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Protein

Aconitate hydratase 3, mitochondrial

Gene

ACO3

Organism
Arabidopsis thaliana (Mouse-ear cress)
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. Contributes to oxidative stress tolerance (PubMed:17013749). Modulates cytosolic citrate metabolism during lipid mobilization. Required during seedling growth (PubMed:25061985).2 Publications

Catalytic activityi

Citrate = isocitrate.By similarity

Cofactori

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

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 2 of the subpathway that synthesizes isocitrate from oxaloacetate.By similarity
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Citrate synthase 5, mitochondrial (CSY5), Citrate synthase 1, peroxisomal (CSY1), Citrate synthase 2, peroxisomal (CSY2), Citrate synthase 3, peroxisomal (CSY3), Citrate synthase 4, mitochondrial (CSY4)
  2. Aconitate hydratase 3, mitochondrial (ACO3), Aconitate hydratase 1 (ACO1), Aconitate hydratase 2, mitochondrial (ACO2)
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)DescriptionActionsGraphical viewLength
Binding sitei182SubstrateBy similarity1
Metal bindingi533Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi599Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi602Iron-sulfur (4Fe-4S)By similarity1
Binding sitei632SubstrateBy similarity1
Binding sitei637SubstrateBy similarity1
Binding sitei795SubstrateBy similarity1

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • aconitate hydratase activity Source: UniProtKB
  • ATP binding Source: TAIR
  • copper ion binding Source: TAIR

GO - Biological processi

  • citrate metabolic process Source: UniProtKB
  • glyoxylate cycle Source: UniProtKB-KW
  • isocitrate metabolic process Source: TAIR
  • response to abscisic acid Source: TAIR
  • response to cadmium ion Source: TAIR
  • response to oxidative stress Source: TAIR
  • response to salt stress Source: TAIR
  • seedling development Source: UniProtKB
  • tricarboxylic acid cycle Source: UniProtKB-UniPathway

Keywordsi

Molecular functionLyase
Biological processGlyoxylate bypass, Tricarboxylic acid cycle
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00223; UER00718.

Names & Taxonomyi

Protein namesi
Recommended name:
Aconitate hydratase 3, mitochondrial1 Publication (EC:4.2.1.3By similarity)
Short name:
Aconitase 31 Publication
Short name:
mACO11 Publication
Alternative name(s):
Citrate hydro-lyase 31 Publication
Gene namesi
Name:ACO31 Publication
Ordered Locus Names:At2g05710Imported
ORF Names:T3P4.5Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRilocus:2063354. AT2G05710.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • vacuolar membrane Source: TAIR

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Reduced cytosolic and mitochondrial aconitase (ACO) activities by 25 and 55 precent, respectively (PubMed:17013749, PubMed:17437406). Increased tolerance to oxidative stress mediated by paraquat, a superoxide-generating agent (PubMed:17013749). Delayed early seedling growth, altered assimilation of acetate feeding and elevated citrate and malate levels (PubMed:25061985).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 78MitochondrionSequence analysisAdd BLAST78
ChainiPRO_000025992179 – 990Aconitate hydratase 3, mitochondrialAdd BLAST912

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei91Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylated at Ser-91 in the cytoplasm; this phosphorylation requires the presence of B'GAMMA.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9SIB9.
PRIDEiQ9SIB9.

PTM databases

iPTMnetiQ9SIB9.

Expressioni

Tissue specificityi

Major aconitase isoenzyme in young seedlings (PubMed:25061985). Expressed in roots, leaves, stems and flowers, and, at low levels, in seeds (PubMed:17437406).2 Publications

Inductioni

Transiently induced during germination.1 Publication

Gene expression databases

ExpressionAtlasiQ9SIB9. baseline and differential.
GenevisibleiQ9SIB9. AT.

Interactioni

Subunit structurei

Monomer (By similarity). Interacts with B'GAMMA in the cytosol (PubMed:25307043).By similarity1 Publication

Protein-protein interaction databases

BioGridi519. 2 interactors.
IntActiQ9SIB9. 1 interactor.
STRINGi3702.AT2G05710.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SIB9.
SMRiQ9SIB9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni301 – 303Substrate bindingBy similarity3
Regioni876 – 877Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0452. Eukaryota.
COG1048. LUCA.
HOGENOMiHOG000025704.
InParanoidiQ9SIB9.
KOiK01681.
OMAiDNISEIR.
OrthoDBiEOG093601QZ.
PhylomeDBiQ9SIB9.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 3 hits.
3.40.1060.10. 1 hit.
InterProiView protein in InterPro
IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR006249. Aconitase/IRP2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiView protein in Pfam
PF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR01341. aconitase_1. 1 hit.
PROSITEiView protein in PROSITE
PS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9SIB9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYLTASSSAS SSIIRAASSR SSSLFSFRSV LSPSVSSTSP SSLLARRSFG
60 70 80 90 100
TISPAFRRWS HSFHSKPSPF RFTSQIRAVS PVLDRLQRTF SSMASEHPFK
110 120 130 140 150
GIFTTLPKPG GGEFGKFYSL PALNDPRVDK LPYSIRILLE SAIRNCDNFQ
160 170 180 190 200
VTKEDVEKII DWEKTSPKQV EIPFKPARVL LQDFTGVPAV VDLACMRDAM
210 220 230 240 250
NKLGSDSNKI NPLVPVDLVI DHSVQVDVAR SENAVQANME LEFQRNKERF
260 270 280 290 300
AFLKWGSTAF QNMLVVPPGS GIVHQVNLEY LGRVVFNTKG LLYPDSVVGT
310 320 330 340 350
DSHTTMIDGL GVAGWGVGGI EAEATMLGQP MSMVLPGVVG FKLAGKMRNG
360 370 380 390 400
VTATDLVLTV TQMLRKHGVV GKFVEFYGNG MSGLSLADRA TIANMSPEYG
410 420 430 440 450
ATMGFFPVDH VTLQYLKLTG RSDETVAMIE AYLRANNMFV DYNEPQQDRV
460 470 480 490 500
YSSYLELNLD DVEPCISGPK RPHDRVTLKE MKADWHSCLD SKVGFKGFAI
510 520 530 540 550
PKEAQEKVVN FSFDGQPAEL KHGSVVIAAI TSCTNTSNPS VMLGAGLVAK
560 570 580 590 600
KACDLGLQVK PWIKTSLAPG SGVVTKYLLK SGLQEYLNEQ GFNIVGYGCT
610 620 630 640 650
TCIGNSGEIN ESVGAAITEN DIVAAAVLSG NRNFEGRVHP LTRANYLASP
660 670 680 690 700
PLVVAYALAG TVNIDFETEP IGKGKNGKDV FLRDIWPTTE EIAEVVQSSV
710 720 730 740 750
LPDMFRATYE SITKGNPMWN KLSVPENTLY SWDPNSTYIH EPPYFKDMTM
760 770 780 790 800
DPPGPHNVKD AYCLLNFGDS ITTDHISPAG NIQKDSPAAK FLMERGVDRK
810 820 830 840 850
DFNSYGSRRG NDEIMARGTF ANIRIVNKLM NGEVGPKTVH IPSGEKLSVF
860 870 880 890 900
DAAMRYKSSG EDTIILAGAE YGSGSSRDWA AKGPMLQGVK AVIAKSFERI
910 920 930 940 950
HRSNLVGMGI IPLCFKSGED ADTLGLTGHE RYTIHLPTDI SEIRPGQDVT
960 970 980 990
VTTDNGKSFT CTVRFDTEVE LAYFNHGGIL PYVIRNLSKQ
Length:990
Mass (Da):108,201
Last modified:November 28, 2006 - v2
Checksum:i552AE563BC2981ED
GO

Sequence cautioni

The sequence AAD25640 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007170 Genomic DNA. Translation: AAD25640.1. Different initiation.
CP002685 Genomic DNA. Translation: AEC05964.1.
AY136414 mRNA. Translation: AAM97080.1.
BT008809 mRNA. Translation: AAP68248.1.
PIRiB84471.
RefSeqiNP_178634.2. NM_126589.3.
UniGeneiAt.26759.
At.67769.

Genome annotation databases

EnsemblPlantsiAT2G05710.1; AT2G05710.1; AT2G05710.
GeneIDi815120.
GrameneiAT2G05710.1; AT2G05710.1; AT2G05710.
KEGGiath:AT2G05710.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007170 Genomic DNA. Translation: AAD25640.1. Different initiation.
CP002685 Genomic DNA. Translation: AEC05964.1.
AY136414 mRNA. Translation: AAM97080.1.
BT008809 mRNA. Translation: AAP68248.1.
PIRiB84471.
RefSeqiNP_178634.2. NM_126589.3.
UniGeneiAt.26759.
At.67769.

3D structure databases

ProteinModelPortaliQ9SIB9.
SMRiQ9SIB9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi519. 2 interactors.
IntActiQ9SIB9. 1 interactor.
STRINGi3702.AT2G05710.1.

PTM databases

iPTMnetiQ9SIB9.

Proteomic databases

PaxDbiQ9SIB9.
PRIDEiQ9SIB9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G05710.1; AT2G05710.1; AT2G05710.
GeneIDi815120.
GrameneiAT2G05710.1; AT2G05710.1; AT2G05710.
KEGGiath:AT2G05710.

Organism-specific databases

AraportiAT2G05710.
TAIRilocus:2063354. AT2G05710.

Phylogenomic databases

eggNOGiKOG0452. Eukaryota.
COG1048. LUCA.
HOGENOMiHOG000025704.
InParanoidiQ9SIB9.
KOiK01681.
OMAiDNISEIR.
OrthoDBiEOG093601QZ.
PhylomeDBiQ9SIB9.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00718.

Miscellaneous databases

PROiQ9SIB9.

Gene expression databases

ExpressionAtlasiQ9SIB9. baseline and differential.
GenevisibleiQ9SIB9. AT.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 3 hits.
3.40.1060.10. 1 hit.
InterProiView protein in InterPro
IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR006249. Aconitase/IRP2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiView protein in Pfam
PF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR01341. aconitase_1. 1 hit.
PROSITEiView protein in PROSITE
PS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiACO3M_ARATH
AccessioniPrimary (citable) accession number: Q9SIB9
Secondary accession number(s): Q8L784
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: March 15, 2017
This is version 112 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.