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Protein

Aconitate hydratase, mitochondrial

Gene

ACO2

Organism
Sus scrofa (Pig)
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.

Catalytic activityi

Citrate = isocitrate.

Cofactori

[4Fe-4S] cluster2 PublicationsNote: Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S] cluster leads to an inactive enzyme.2 Publications

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 – 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

GO - Biological processi

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. 6170.
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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionAdd
BLAST
Chaini28 – 781754Aconitate hydratase, mitochondrialPRO_0000000543Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281Pyrrolidone carboxylic acid1 Publication
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 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 residuei739 – 7391N6-acetyllysineBy similarity
Modified residuei743 – 7431N6-acetyllysineBy similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiP16276.
PeptideAtlasiP16276.
PRIDEiP16276.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000000070.

Structurei

Secondary structure

1
781
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 strandi87 – 915Combined sources
Beta strandi94 – 996Combined sources
Helixi100 – 11314Combined 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 – 2178Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi228 – 2369Combined sources
Helixi244 – 25512Combined sources
Turni257 – 2626Combined 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 – 3264Combined 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 – 3827Combined 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
Turni617 – 6204Combined sources
Beta strandi621 – 6233Combined sources
Turni624 – 6274Combined sources
Beta strandi628 – 6303Combined sources
Turni635 – 6373Combined sources
Helixi643 – 65210Combined sources
Beta strandi657 – 6604Combined sources
Beta strandi663 – 6653Combined sources
Beta strandi667 – 6693Combined 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
1B0JX-ray2.50A28-781[»]
1B0KX-ray2.50A29-781[»]
1B0MX-ray2.50A29-781[»]
5ACNX-ray2.10A29-781[»]
6ACNX-ray2.50A29-781[»]
7ACNX-ray2.00A29-781[»]
ProteinModelPortaliP16276.
SMRiP16276. Positions 29-781.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16276.

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

eggNOGiKOG0453. Eukaryota.
COG1048. LUCA.
HOGENOMiHOG000224293.
HOVERGENiHBG000248.
InParanoidiP16276.
KOiK01681.

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.

P16276-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPYSLLVTR LQKALGVRQY HVASVLCQRA KVAMSHFEPH EYIRYDLLEK
60 70 80 90 100
NIDIVRKRLN 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 EFKDHLVPDP GCHYDQVIEI NLSELKPHIN
360 370 380 390 400
GPFTPDLAHP VAEVGSVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA
410 420 430 440 450
KQALAHGLKC KSQFTITPGS EQIRATIERD GYAQVLRDVG 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
SSGQRVDVSP TSQRLQLLEP FDKWDGKDLE DLQILIKVKG KCTTDHISAA
610 620 630 640 650
GPWLKFRGHL DNISNNLLIG AINIENRKAN SVRNAVTQEF GPVPDTARYY
660 670 680 690 700
KQHGIRWVVI GDENYGEGSS REHRALEPRH LGGRAIITKS FARIHETNLK
710 720 730 740 750
KQGLLPLTFA DPADYNKIHP VDKLTIQGLK DFAPGKPLKC IIKHPNGTQE
760 770 780
TILLNHTFNE TQIEWFRAGS ALNRMKELQQ K
Length:781
Mass (Da):85,761
Last modified:August 1, 1990 - v1
Checksum:i5737FD9BCFCEF184
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05224 mRNA. Translation: AAA30987.1.
PIRiA35544.
RefSeqiNP_999119.1. NM_213954.1.
UniGeneiSsc.4263.

Genome annotation databases

GeneIDi396999.
KEGGissc:396999.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05224 mRNA. Translation: AAA30987.1.
PIRiA35544.
RefSeqiNP_999119.1. NM_213954.1.
UniGeneiSsc.4263.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B0JX-ray2.50A28-781[»]
1B0KX-ray2.50A29-781[»]
1B0MX-ray2.50A29-781[»]
5ACNX-ray2.10A29-781[»]
6ACNX-ray2.50A29-781[»]
7ACNX-ray2.00A29-781[»]
ProteinModelPortaliP16276.
SMRiP16276. Positions 29-781.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000000070.

Proteomic databases

PaxDbiP16276.
PeptideAtlasiP16276.
PRIDEiP16276.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396999.
KEGGissc:396999.

Organism-specific databases

CTDi50.

Phylogenomic databases

eggNOGiKOG0453. Eukaryota.
COG1048. LUCA.
HOGENOMiHOG000224293.
HOVERGENiHBG000248.
InParanoidiP16276.
KOiK01681.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00718.
BRENDAi4.2.1.3. 6170.

Miscellaneous databases

EvolutionaryTraceiP16276.

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

  1. "Cloning and structural characterization of porcine heart aconitase."
    Zheng L., Andrews P.C., Hermodson M.A., Dixon J.E., Zalkin H.
    J. Biol. Chem. 265:2814-2821(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Heart.
  2. "Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal."
    Robbins A.H., Stout C.D.
    Proc. Natl. Acad. Sci. U.S.A. 86:3639-3643(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 29-781 IN COMPLEX WITH IRON-SULFUR, COFACTOR.
    Tissue: Heart.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  4. "The mechanism of aconitase: 1.8 A resolution crystal structure of the S642A:citrate complex."
    Lloyd S.J., Lauble H., Prasad G.S., Stout C.D.
    Protein Sci. 8:2655-2662(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 29-779 OF MUTANT ALA-669 IN COMPLEX WITH IRON-SULFUR; THE SUBSTRATE CITRATE AND ISOCITRATE, COFACTOR, REACTION MECHANISM.

Entry informationi

Entry nameiACON_PIG
AccessioniPrimary (citable) accession number: P16276
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: July 6, 2016
This is version 129 of the entry and version 1 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

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.