Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aconitate hydratase, mitochondrial

Gene

Aco2

Organism
Rattus norvegicus (Rat)
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. Binding of a [3Fe-4S] cluster leads to an inactive enzyme.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, mitochondrial (Cs)
  2. Aconitate hydratase, 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991SubstrateBy 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 sitei474 – 4741SubstrateBy similarity
Binding sitei479 – 4791SubstrateBy similarity
Binding sitei607 – 6071SubstrateBy similarity

GO - Molecular functioni

  • 3 iron, 4 sulfur cluster binding Source: RGD
  • 4 iron, 4 sulfur cluster binding Source: RGD
  • aconitate hydratase activity Source: RGD
  • iron ion binding Source: Ensembl

GO - Biological processi

  • citrate metabolic process Source: RGD
  • isocitrate metabolic process Source: RGD
  • tricarboxylic acid cycle Source: RGD
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

BRENDAi4.2.1.3. 5301.
ReactomeiR-RNO-71403. Citric acid cycle (TCA cycle).
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:Aco2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi621360. Aco2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: RGD
  • myelin sheath Source: Ensembl
  • nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionBy similarityAdd
BLAST
Chaini28 – 780753Aconitate hydratase, mitochondrialPRO_0000000544Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281Pyrrolidone carboxylic acidBy similarity
Modified residuei31 – 311N6-succinyllysineBy similarity
Modified residuei50 – 501N6-acetyllysine; alternateBy similarity
Modified residuei50 – 501N6-succinyllysine; alternateBy similarity
Modified residuei138 – 1381N6-acetyllysine; alternateBy similarity
Modified residuei138 – 1381N6-succinyllysine; alternateBy similarity
Modified residuei144 – 1441N6-acetyllysine; alternateBy similarity
Modified residuei144 – 1441N6-succinyllysine; alternateBy similarity
Cross-linki144 – 144Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei233 – 2331N6-acetyllysine; alternateBy similarity
Modified residuei233 – 2331N6-succinyllysine; alternateBy similarity
Modified residuei411 – 4111N6-succinyllysineBy similarity
Modified residuei517 – 5171N6-acetyllysine; alternateBy similarity
Modified residuei517 – 5171N6-succinyllysine; alternateBy similarity
Modified residuei523 – 5231N6-acetyllysine; alternateBy similarity
Modified residuei523 – 5231N6-succinyllysine; alternateBy similarity
Modified residuei549 – 5491N6-succinyllysineBy similarity
Modified residuei559 – 5591PhosphoserineCombined sources
Modified residuei573 – 5731N6-acetyllysine; alternateBy similarity
Modified residuei573 – 5731N6-succinyllysine; alternateBy similarity
Modified residuei577 – 5771N6-succinyllysineBy similarity
Modified residuei591 – 5911N6-succinyllysineBy similarity
Modified residuei605 – 6051N6-acetyllysine; alternateBy similarity
Modified residuei605 – 6051N6-succinyllysine; alternateBy similarity
Modified residuei628 – 6281N6-succinyllysineBy similarity
Modified residuei670 – 6701PhosphoserineBy similarity
Modified residuei689 – 6891N6-succinyllysineBy similarity
Modified residuei723 – 7231N6-acetyllysine; alternateBy similarity
Modified residuei723 – 7231N6-succinyllysine; alternateBy similarity
Modified residuei730 – 7301N6-acetyllysine; alternateBy similarity
Modified residuei730 – 7301N6-succinyllysine; alternateBy similarity
Modified residuei736 – 7361N6-acetyllysineBy similarity
Modified residuei743 – 7431N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Pyrrolidone carboxylic acid, Ubl conjugation

Proteomic databases

PaxDbiQ9ER34.
PRIDEiQ9ER34.

2D gel databases

World-2DPAGE0004:Q9ER34.

PTM databases

iPTMnetiQ9ER34.
PhosphoSiteiQ9ER34.

Expressioni

Gene expression databases

GenevisibleiQ9ER34. RN.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi249448. 1 interaction.
IntActiQ9ER34. 1 interaction.
STRINGi10116.ENSRNOP00000029144.

Structurei

3D structure databases

ProteinModelPortaliQ9ER34.
SMRiQ9ER34. Positions 29-780.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni192 – 1943Substrate bindingBy similarity
Regioni670 – 6712Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0453. Eukaryota.
COG1048. LUCA.
GeneTreeiENSGT00840000129913.
HOGENOMiHOG000224293.
HOVERGENiHBG000248.
InParanoidiQ9ER34.
KOiK01681.
OMAiPLKCIIK.
OrthoDBiEOG74FF06.
PhylomeDBiQ9ER34.
TreeFamiTF300627.

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.

Q9ER34-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPYSLLVTR LQKALGVRQY HVASALCQRA KVAMSHFEPS EYIRYDLLEK
60 70 80 90 100
NINIVRKRLN RPLTLSEKIV YGHLDDPANQ EIERGKTYLR LRPDRVAMQD
110 120 130 140 150
ATAQMAMLQF ISSGLPKVAV PSTIHCDHLI EAQLGGEKDL RRAKDINQEV
160 170 180 190 200
YNFLATAGAK YGVGFWRPGS GIIHQIILEN YAYPGVLLIG TDSHTPNGGG
210 220 230 240 250
LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGTLSG WTSPKDVILK
260 270 280 290 300
VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN
310 320 330 340 350
HRMKKYLSKT GRADIANLAE EFKDHLVPDP GCQYDQVIEI NLNELKPHIN
360 370 380 390 400
GPFTPDLAHP VADVGTVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA
410 420 430 440 450
KQALAHGLKC KSQFTITPGS EQIRATIERD GYAQILRDVG GIVLANACGP
460 470 480 490 500
CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN DANPETHAFV TSPEIVTALA
510 520 530 540 550
IAGTLKFNPE TDFLTGKDGK KFKLEAPDAD ELPRSDFDPG QDTYQHPPKD
560 570 580 590 600
SSGQRVDVSP TSQRLQLLEP FDKWDGKDLE DLQILIKVKG KCTTDHISAA
610 620 630 640 650
GPWLKFRGHL DNISNNLLIG AINIENGKAN SVRNAVTQEF GPVPDTARYY
660 670 680 690 700
KKHGIRWVVI GDENYGEGSS REHAALEPRH LGGRAIITKS FARIHETNLK
710 720 730 740 750
KQGLLPLTFA DPSDYNKIHP VDKLTIQGLK DFAPGKPLNC IIKHPNGTQE
760 770 780
TILLNHTFNE TQIEWFRAGS ALNRMKELQQ
Length:780
Mass (Da):85,433
Last modified:February 1, 2005 - v2
Checksum:iE523564299DD38BD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti224 – 2241L → P in CAC11018 (Ref. 1) Curated
Sequence conflicti295 – 2951S → P in CAC11018 (Ref. 1) Curated
Sequence conflicti582 – 5821L → Q in CAC11018 (Ref. 1) Curated
Sequence conflicti659 – 6591V → M in CAC11018 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243266 mRNA. Translation: CAC11018.1.
BC061999 mRNA. Translation: AAH61999.1.
RefSeqiNP_077374.2. NM_024398.2.
UniGeneiRn.43737.

Genome annotation databases

EnsembliENSRNOT00000038612; ENSRNOP00000029144; ENSRNOG00000024128.
GeneIDi79250.
KEGGirno:79250.
UCSCiRGD:621360. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243266 mRNA. Translation: CAC11018.1.
BC061999 mRNA. Translation: AAH61999.1.
RefSeqiNP_077374.2. NM_024398.2.
UniGeneiRn.43737.

3D structure databases

ProteinModelPortaliQ9ER34.
SMRiQ9ER34. Positions 29-780.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249448. 1 interaction.
IntActiQ9ER34. 1 interaction.
STRINGi10116.ENSRNOP00000029144.

PTM databases

iPTMnetiQ9ER34.
PhosphoSiteiQ9ER34.

2D gel databases

World-2DPAGE0004:Q9ER34.

Proteomic databases

PaxDbiQ9ER34.
PRIDEiQ9ER34.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000038612; ENSRNOP00000029144; ENSRNOG00000024128.
GeneIDi79250.
KEGGirno:79250.
UCSCiRGD:621360. rat.

Organism-specific databases

CTDi50.
RGDi621360. Aco2.

Phylogenomic databases

eggNOGiKOG0453. Eukaryota.
COG1048. LUCA.
GeneTreeiENSGT00840000129913.
HOGENOMiHOG000224293.
HOVERGENiHBG000248.
InParanoidiQ9ER34.
KOiK01681.
OMAiPLKCIIK.
OrthoDBiEOG74FF06.
PhylomeDBiQ9ER34.
TreeFamiTF300627.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00718.
BRENDAi4.2.1.3. 5301.
ReactomeiR-RNO-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

NextBioi614724.
PROiQ9ER34.

Gene expression databases

GenevisibleiQ9ER34. RN.

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. "Molecular cloning of the rat heart mitochondrial aconitase."
    Wieland A., Bruss M.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 32-44; 59-84; 96-138; 143-160; 234-245; 251-302; 313-323; 371-395; 402-409; 412-424; 430-458; 466-474; 480-517; 522-587; 592-628; 634-648; 657-679 AND 694-767, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACON_RAT
AccessioniPrimary (citable) accession number: Q9ER34
Secondary accession number(s): Q6P6V3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: May 11, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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.