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P20004

- ACON_BOVIN

UniProt

P20004 - ACON_BOVIN

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Protein

Aconitate hydratase, mitochondrial

Gene

ACO2

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.

Catalytic activityi

Citrate = isocitrate.

Cofactori

[4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S] cluster leads to an inactive enzyme.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991Substrate
Metal bindingi385 – 3851Iron-sulfur (4Fe-4S)2 Publications
Metal bindingi448 – 4481Iron-sulfur (4Fe-4S)2 Publications
Metal bindingi451 – 4511Iron-sulfur (4Fe-4S)2 Publications
Binding sitei474 – 4741Substrate
Binding sitei479 – 4791Substrate
Binding sitei607 – 6071Substrate

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. aconitate hydratase activity Source: AgBase
  3. iron ion binding Source: AgBase

GO - Biological processi

  1. citrate metabolic process Source: AgBase
  2. tricarboxylic acid cycle Source: AgBase
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

ReactomeiREACT_227707. 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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 5

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: AgBase
  2. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionAdd
BLAST
Chaini28 – 780753Aconitate hydratase, mitochondrialPRO_0000000540Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281Pyrrolidone carboxylic acid
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 – 5591PhosphoserineBy similarity
Modified residuei573 – 5731N6-acetyllysine; alternateBy similarity
Modified residuei573 – 5731N6-succinyllysine; alternateBy similarity
Modified residuei591 – 5911N6-succinyllysineBy similarity
Modified residuei605 – 6051N6-acetyllysine; alternateBy similarity
Modified residuei605 – 6051N6-succinyllysine; alternateBy similarity
Modified residuei628 – 6281N6-succinyllysineBy 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

PaxDbiP20004.
PRIDEiP20004.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiP20004. 1 interaction.

Structurei

Secondary structure

1
780
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 353Combined sources
Beta strandi38 – 425Combined sources
Helixi45 – 5915Combined sources
Helixi65 – 717Combined sources
Turni77 – 793Combined sources
Turni84 – 863Combined sources
Beta strandi88 – 914Combined sources
Beta strandi94 – 996Combined sources
Turni100 – 1023Combined sources
Helixi103 – 11311Combined sources
Beta strandi122 – 1254Combined sources
Beta strandi132 – 1343Combined sources
Helixi136 – 14611Combined sources
Helixi148 – 16114Combined sources
Beta strandi164 – 1663Combined sources
Helixi173 – 1808Combined sources
Beta strandi187 – 1926Combined sources
Helixi195 – 2017Combined sources
Beta strandi204 – 2074Combined sources
Helixi210 – 2189Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi228 – 2369Combined sources
Helixi244 – 25512Combined sources
Turni256 – 2627Combined sources
Beta strandi263 – 2697Combined sources
Helixi270 – 2745Combined sources
Helixi277 – 28610Combined sources
Helixi287 – 2904Combined sources
Beta strandi293 – 2964Combined sources
Helixi301 – 3099Combined sources
Helixi313 – 3219Combined sources
Helixi323 – 3253Combined sources
Beta strandi335 – 3417Combined sources
Helixi342 – 3443Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi352 – 3543Combined sources
Beta strandi358 – 3603Combined sources
Helixi361 – 37111Combined sources
Beta strandi376 – 3838Combined sources
Turni384 – 3863Combined sources
Helixi390 – 40415Combined sources
Turni405 – 4073Combined sources
Beta strandi411 – 4166Combined sources
Helixi421 – 4299Combined sources
Helixi432 – 4387Combined sources
Beta strandi441 – 4433Combined sources
Helixi449 – 4524Combined sources
Beta strandi466 – 4738Combined sources
Turni477 – 4815Combined sources
Beta strandi486 – 4905Combined sources
Helixi493 – 50210Combined sources
Beta strandi504 – 5063Combined sources
Turni509 – 5113Combined sources
Beta strandi513 – 5153Combined sources
Beta strandi521 – 5233Combined sources
Turni549 – 5513Combined sources
Beta strandi563 – 5653Combined sources
Beta strandi579 – 58810Combined sources
Helixi594 – 5974Combined sources
Helixi601 – 6066Combined sources
Helixi610 – 6134Combined sources
Helixi614 – 6163Combined sources
Turni618 – 6203Combined sources
Beta strandi621 – 6233Combined sources
Turni624 – 6263Combined sources
Turni635 – 6373Combined sources
Helixi643 – 65210Combined sources
Beta strandi657 – 6604Combined sources
Beta strandi663 – 6653Combined sources
Helixi673 – 6808Combined sources
Beta strandi683 – 6897Combined sources
Helixi693 – 7019Combined sources
Beta strandi705 – 7117Combined sources
Helixi712 – 7176Combined sources
Beta strandi723 – 7275Combined sources
Helixi729 – 7313Combined sources
Beta strandi738 – 7436Combined sources
Beta strandi749 – 7557Combined sources
Helixi760 – 7689Combined sources
Helixi771 – 7788Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ACOX-ray2.05A29-779[»]
1AMIX-ray2.00A28-780[»]
1AMJX-ray2.00A28-780[»]
1C96X-ray1.81A29-779[»]
1C97X-ray1.98A29-779[»]
1FGHX-ray2.05A29-779[»]
1NISX-ray2.05A29-779[»]
1NITX-ray2.05A29-779[»]
8ACNX-ray2.00A29-780[»]
ProteinModelPortaliP20004.
SMRiP20004. Positions 29-780.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20004.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1048.
GeneTreeiENSGT00760000119287.
HOGENOMiHOG000224293.
HOVERGENiHBG000248.
InParanoidiP20004.
KOiK01681.
OMAiPLKCIIK.
OrthoDBiEOG74FF06.
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.

P20004-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPYSLLVSR LQKALGARQY HVASVLCQRA KVAMSHFEPN 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 GVKLTGSLSG WTSPKDVILK
260 270 280 290 300
VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN
310 320 330 340 350
HRMKKYLSKT GRADIANLAD EFKDHLVPDS GCHYDQLIEI NLSELKPHIN
360 370 380 390 400
GPFTPDLAHP VAEVGSVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA
410 420 430 440 450
KQALAHGLQC KSQFTITPGS EQIRATIERD GYAQILRDVG GIVLANACGP
460 470 480 490 500
CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN DANPETHAFV TSPEIVTALA
510 520 530 540 550
IAGTLKFNPE TDFLTGKDGK KFKLEAPDAD ELPRAEFDPG QDTYQHPPKD
560 570 580 590 600
SSGQQVDVSP TSQRLQLLEP FDKWDGRDLE DLQILIKVKG KCTTDHISAA
610 620 630 640 650
GPWLKFRGHL DNISNNLLIG AINVENGKAN SVRNAVTQEF GPVPDTARYY
660 670 680 690 700
KKHGIRWVVI GDENYGEGSS REHAALEPRH LGGRAIITKS FARIHETNLK
710 720 730 740 750
KQGLLPLTFA DPADYNKIHP VDKLTIKGLK DFAPGKPLTC IIKHPNGTQE
760 770 780
TILLNHTFNE TQIEWFRAGS ALNRMKELQK
Length:780
Mass (Da):85,359
Last modified:July 11, 2006 - v4
Checksum:i91EB21B3923F16C5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401N → H AA sequence (PubMed:3372519)Curated
Sequence conflicti53 – 531N → D AA sequence (PubMed:3372519)Curated
Sequence conflicti99 – 991Q → R in CAA90177. 1 PublicationCurated
Sequence conflicti179 – 1791E → G in AAI02643. 1 PublicationCurated
Sequence conflicti217 – 2171M → T in CAA90177. 1 PublicationCurated
Sequence conflicti409 – 4091Q → K AA sequence (PubMed:3372519)Curated
Sequence conflicti435 – 4351I → V AA sequence (PubMed:3372519)Curated
Sequence conflicti555 – 5551Q → R AA sequence (PubMed:3372519)Curated
Sequence conflicti577 – 5771R → K AA sequence (PubMed:3372519)Curated
Sequence conflicti624 – 6241V → S AA sequence (PubMed:3372519)Curated
Sequence conflicti627 – 6271G → R AA sequence (PubMed:3372519)Curated
Sequence conflicti652 – 6521K → Q AA sequence (PubMed:3372519)Curated
Sequence conflicti674 – 6741A → S AA sequence (PubMed:3372519)Curated
Sequence conflicti680 – 6801H → F AA sequence (PubMed:3372519)Curated
Sequence conflicti727 – 7271K → Q AA sequence (PubMed:3372519)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49931 mRNA. Translation: CAA90177.1.
BC102642 mRNA. Translation: AAI02643.1.
PIRiS57528.
RefSeqiNP_776402.1. NM_173977.3.
UniGeneiBt.5210.

Genome annotation databases

EnsembliENSBTAT00000008431; ENSBTAP00000008431; ENSBTAG00000006429.
GeneIDi280976.
KEGGibta:280976.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49931 mRNA. Translation: CAA90177.1 .
BC102642 mRNA. Translation: AAI02643.1 .
PIRi S57528.
RefSeqi NP_776402.1. NM_173977.3.
UniGenei Bt.5210.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ACO X-ray 2.05 A 29-779 [» ]
1AMI X-ray 2.00 A 28-780 [» ]
1AMJ X-ray 2.00 A 28-780 [» ]
1C96 X-ray 1.81 A 29-779 [» ]
1C97 X-ray 1.98 A 29-779 [» ]
1FGH X-ray 2.05 A 29-779 [» ]
1NIS X-ray 2.05 A 29-779 [» ]
1NIT X-ray 2.05 A 29-779 [» ]
8ACN X-ray 2.00 A 29-780 [» ]
ProteinModelPortali P20004.
SMRi P20004. Positions 29-780.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P20004. 1 interaction.

Proteomic databases

PaxDbi P20004.
PRIDEi P20004.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000008431 ; ENSBTAP00000008431 ; ENSBTAG00000006429 .
GeneIDi 280976.
KEGGi bta:280976.

Organism-specific databases

CTDi 50.

Phylogenomic databases

eggNOGi COG1048.
GeneTreei ENSGT00760000119287.
HOGENOMi HOG000224293.
HOVERGENi HBG000248.
InParanoidi P20004.
KOi K01681.
OMAi PLKCIIK.
OrthoDBi EOG74FF06.
TreeFami TF300627.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00718 .
Reactomei REACT_227707. Citric acid cycle (TCA cycle).

Miscellaneous databases

EvolutionaryTracei P20004.
NextBioi 20805079.

Family and domain databases

Gene3Di 3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProi IPR015931. 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 ]
PANTHERi PTHR11670. PTHR11670. 1 hit.
Pfami PF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view ]
PRINTSi PR00415. ACONITASE.
SUPFAMi SSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsi TIGR01340. aconitase_mito. 1 hit.
PROSITEi PS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Xu N., Liu W., Woldegiogis G., Sun X.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  3. "Identification of the reactive sulfhydryl and sequences of cysteinyl-tryptic peptides from beef heart aconitase."
    Plank D.W., Howard J.B.
    J. Biol. Chem. 263:8184-8189(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 28-780.
    Tissue: Heart.
  4. "Cysteine labeling studies of beef heart aconitase containing a 4Fe, a cubane 3Fe, or a linear 3Fe cluster."
    Plank D.W., Kennedy M.C., Beinert H., Howard J.B.
    J. Biol. Chem. 264:20385-20393(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 118-139 AND 439-457, CHARACTERIZATION OF IRON-SULFUR CLUSTERS.
    Tissue: Heart.
  5. "Crystal structures of aconitase with isocitrate and nitroisocitrate bound."
    Lauble H., Kennedy M.C., Beinert H., Stout C.D.
    Biochemistry 31:2735-2748(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-779 IN COMPLEX WITH IRON-SULFUR AND THE SUBSTRATE ANALOG NITROISOCITRATE, COFACTOR, REACTION MECHANISM.

Entry informationi

Entry nameiACON_BOVIN
AccessioniPrimary (citable) accession number: P20004
Secondary accession number(s): Q3SZZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 11, 2006
Last modified: November 26, 2014
This is version 134 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3