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Protein

Aconitate hydratase 1

Gene

ACO1

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.By similarity

Catalytic activityi

Citrate = isocitrate.

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.
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 2, mitochondrial (ACO2), Aconitate hydratase 1 (ACO1), Aconitate hydratase 3, mitochondrial (ACO3)
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 sitei90 – 901SubstrateBy similarity
Metal bindingi441 – 4411Iron-sulfur (4Fe-4S)By similarity
Metal bindingi507 – 5071Iron-sulfur (4Fe-4S)By similarity
Metal bindingi510 – 5101Iron-sulfur (4Fe-4S)By similarity
Binding sitei540 – 5401SubstrateBy similarity
Binding sitei545 – 5451SubstrateBy similarity
Binding sitei703 – 7031SubstrateBy similarity

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • aconitate hydratase activity Source: TAIR
  • copper ion binding Source: TAIR
  • mRNA 5'-UTR binding Source: TAIR

GO - Biological processi

  • citrate metabolic process Source: TAIR
  • isocitrate metabolic process Source: TAIR
  • response to salt stress Source: TAIR
  • tricarboxylic acid cycle Source: UniProtKB-UniPathway
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

BioCyciARA:GQT-152-MONOMER.
MetaCyc:AT4G35830-MONOMER.
UniPathwayiUPA00223; UER00718.

Names & Taxonomyi

Protein namesi
Recommended name:
Aconitate hydratase 1 (EC:4.2.1.3)
Short name:
Aconitase 1
Alternative name(s):
Citrate hydro-lyase 1
Gene namesi
Name:ACO1
Synonyms:ACO
Ordered Locus Names:At4g35830
ORF Names:F4B14.100
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G35830.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • cytosol Source: TAIR
  • mitochondrion Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 898897Aconitate hydratase 1PRO_0000076651Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ42560.
PRIDEiQ42560.

PTM databases

iPTMnetiQ42560.

Expressioni

Gene expression databases

ExpressionAtlasiQ42560. baseline and differential.
GenevisibleiQ42560. AT.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi15019. 2 interactions.
IntActiQ42560. 1 interaction.
STRINGi3702.AT4G35830.1.

Structurei

3D structure databases

ProteinModelPortaliQ42560.
SMRiQ42560. Positions 5-897.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni209 – 2113Substrate bindingBy similarity
Regioni784 – 7852Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Phylogenomic databases

eggNOGiKOG0452. Eukaryota.
COG1048. LUCA.
HOGENOMiHOG000025704.
InParanoidiQ42560.
KOiK01681.
OMAiETGQVYD.
PhylomeDBiQ42560.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 3 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.
IPR006249. Aconitase/IRP2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 4 hits.
PfamiPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR01341. aconitase_1. 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.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q42560-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASENPFRSI LKALEKPDGG EFGNYYSLPA LNDPRIDKLP YSIRILLESA
60 70 80 90 100
IRNCDEFQVK SKDVEKILDW ENTSPKQVEI PFKPARVLLQ DFTGVPAVVD
110 120 130 140 150
LACMRDAMNN LGGDSNKINP LVPVDLVIDH SVQVDVARSE NAVQANMELE
160 170 180 190 200
FQRNKERFAF LKWGSNAFHN MLVVPPGSGI VHQVNLEYLA RVVFNTNGLL
210 220 230 240 250
YPDSVVGTDS HTTMIDGLGV AGWGVGGIEA EATMLGQPMS MVLPGVVGFK
260 270 280 290 300
LTGKLRDGMT ATDLVLTVTQ MLRKHGVVGK FVEFHGEGMR ELSLADRATI
310 320 330 340 350
ANMSPEYGAT MGFFPVDHVT LQYLRLTGRS DDTVSMIEAY LRANKMFVDY
360 370 380 390 400
SEPESKTVYS SCLELNLEDV EPCVSGPKRP HDRVPLKEMK ADWHSCLDNR
410 420 430 440 450
VGFKGFAVPK EAQSKAVEFN FNGTTAQLRH GDVVIAAITS CTNTSNPSVM
460 470 480 490 500
LGAALVAKKA CDLGLEVKPW IKTSLAPGSG VVTKYLAKSG LQKYLNQLGF
510 520 530 540 550
SIVGYGCTTC IGNSGDIHEA VASAIVDNDL VASAVLSGNR NFEGRVHPLT
560 570 580 590 600
RANYLASPPL VVAYALAGTV DIDFETQPIG TGKDGKQIFF RDIWPSNKEV
610 620 630 640 650
AEVVQSSVLP DMFKATYEAI TKGNSMWNQL SVASGTLYEW DPKSTYIHEP
660 670 680 690 700
PYFKGMTMSP PGPHGVKDAY CLLNFGDSIT TDHISPAGSI HKDSPAAKYL
710 720 730 740 750
MERGVDRRDF NSYGSRRGND EIMARGTFAN IRIVNKHLKG EVGPKTVHIP
760 770 780 790 800
TGEKLSVFDA AMKYRNEGRD TIILAGAEYG SGSSRDWAAK GPMLLGVKAV
810 820 830 840 850
ISKSFERIHR SNLVGMGIIP LCFKAGEDAE TLGLTGQELY TIELPNNVSE
860 870 880 890
IKPGQDVTVV TNNGKSFTCT LRFDTEVELA YFDHGGILQY VIRNLIKQ
Length:898
Mass (Da):98,152
Last modified:February 21, 2001 - v2
Checksum:iD90457C4FB0B56B8
GO

Sequence cautioni

The sequence CAA58046.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301H → Y in CAA58046 (PubMed:7713917).Curated
Sequence conflicti232 – 2332AT → RP in CAA58046 (PubMed:7713917).Curated
Sequence conflicti715 – 72713SRRGN…MARGT → VAVVMMRLWREH (PubMed:7713917).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82839 mRNA. Translation: CAA58046.1. Different initiation.
AL031986 Genomic DNA. Translation: CAA21469.1.
AL161588 Genomic DNA. Translation: CAB81492.1.
CP002687 Genomic DNA. Translation: AEE86576.1.
AY062772 mRNA. Translation: AAL32850.1.
PIRiT04693.
RefSeqiNP_195308.1. NM_119749.3. [Q42560-1]
UniGeneiAt.24717.

Genome annotation databases

EnsemblPlantsiAT4G35830.1; AT4G35830.1; AT4G35830. [Q42560-1]
GeneIDi829737.
KEGGiath:AT4G35830.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82839 mRNA. Translation: CAA58046.1. Different initiation.
AL031986 Genomic DNA. Translation: CAA21469.1.
AL161588 Genomic DNA. Translation: CAB81492.1.
CP002687 Genomic DNA. Translation: AEE86576.1.
AY062772 mRNA. Translation: AAL32850.1.
PIRiT04693.
RefSeqiNP_195308.1. NM_119749.3. [Q42560-1]
UniGeneiAt.24717.

3D structure databases

ProteinModelPortaliQ42560.
SMRiQ42560. Positions 5-897.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi15019. 2 interactions.
IntActiQ42560. 1 interaction.
STRINGi3702.AT4G35830.1.

PTM databases

iPTMnetiQ42560.

Proteomic databases

PaxDbiQ42560.
PRIDEiQ42560.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G35830.1; AT4G35830.1; AT4G35830. [Q42560-1]
GeneIDi829737.
KEGGiath:AT4G35830.

Organism-specific databases

TAIRiAT4G35830.

Phylogenomic databases

eggNOGiKOG0452. Eukaryota.
COG1048. LUCA.
HOGENOMiHOG000025704.
InParanoidiQ42560.
KOiK01681.
OMAiETGQVYD.
PhylomeDBiQ42560.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00718.
BioCyciARA:GQT-152-MONOMER.
MetaCyc:AT4G35830-MONOMER.

Miscellaneous databases

PROiQ42560.

Gene expression databases

ExpressionAtlasiQ42560. baseline and differential.
GenevisibleiQ42560. AT.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 3 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.
IPR006249. Aconitase/IRP2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 4 hits.
PfamiPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR01341. aconitase_1. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure, genomic organization, and expression of the Arabidopsis thaliana aconitase gene. Plant aconitase show significant homology with mammalian iron-responsive element-binding protein."
    Peyret P., Perez P., Alric M.
    J. Biol. Chem. 270:8131-8137(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Proteomic approach to identify novel mitochondrial proteins in Arabidopsis."
    Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.
    Plant Physiol. 127:1694-1710(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 44-52 AND 472-485.
    Tissue: Leaf and Stem.
  6. "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
    Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
    Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.
  7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACO1_ARATH
AccessioniPrimary (citable) accession number: Q42560
Secondary accession number(s): Q9SZT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 21, 2001
Last modified: June 8, 2016
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.