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Reviewed, UniProtKB/Swiss-Prot Q90875 (ACOC_CHICK)

Last modified September 1, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cytoplasmic aconitate hydratase
      Short name=Aconitase
    EC=4.2.1.3
Alternative name(s):
    Citrate hydro-lyase
    Iron-responsive element-binding protein 1
      Short name=IRE-BP 1
Gene names
Name: ACO1
Synonyms: IREB1
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length889 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA By similarity. This protein also expresses aconitase activity By similarity.

Catalytic activity

Citrate = isocitrate.

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
RNA-binding
   Molecular functionLyase
Gene Ontology (GO)
   Biological processtricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

aconitate hydratase activity

Inferred from electronic annotation. Source: EC

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 889889Cytoplasmic aconitate hydratase
PRO_0000076679

Sites

Metal binding4371Iron-sulfur (4Fe-4S) By similarity
Metal binding5031Iron-sulfur (4Fe-4S) By similarity
Metal binding5061Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q90875-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 527314F6AE08C842

FASTA88998,074
        10         20         30         40         50         60 
MSNPFVQIVE PLDAKEPVKK FFNLSKLEDV RYARLPFSIR VLLEAAIRNC DEFLVKKQDV 

        70         80         90        100        110        120 
ENILNWKVMQ HKNVEVPFKP ARVILQDFTG VPAVVDFAAM RDAVKKLGGD PEKINPICPA 

       130        140        150        160        170        180 
DLVIDHSIQV DFNRRSDSLQ KNQDLEFERN KERFEFLKWG SQAFKNMRII PPGSGIIHQV 

       190        200        210        220        230        240 
NLEYLARVVM DQDGYYYPDS VVGTDSHTTM VDGLGVLGWG VGGIEAEAVM LGQPISMVLP 

       250        260        270        280        290        300 
EVVGYKLLGN PQPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC 

       310        320        330        340        350        360 
PEYGATAAYF PVDDISIGYL VQTGRDKEKV LCTKKYLEAV GMLRDFKNSS QDPDFTQVVE 

       370        380        390        400        410        420 
LDLHTVVPCC SGPKRPQDKV AVSDMKKDFE TCLGAKQGFK GFQIAPDRHN SVIKFNFEGC 

       430        440        450        460        470        480 
DFELAHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVEAG LTVKPYIKTS LSPGSGVVTY 

       490        500        510        520        530        540 
YLRESGVMSY LSQLGFDVVG YGCMTCIGNS GPLPDSVVEA ITQGDLVAVG VLSGNRNFEG 

       550        560        570        580        590        600 
RVHPNTRANY LASPPLVIAY AIAGTVRIDF EKEPLGISAS GKKIFLKDIW PTRNEIQAVE 

       610        620        630        640        650        660 
RQYVIPGMFK EVYQKIETVN EAWNALDAPS DKLYTWNPKS TYIKSPPFFD GLTLALQTPK 

       670        680        690        700        710        720 
TIEDAYVLLN FGDSVTTDHI SPAGNIARNS PAARYLTSRG LTPREFNSYG SRRGNDAVMA 

       730        740        750        760        770        780 
RGTFANIRLV NKFIDKQGPQ TIHFPSGETL DVFDAAERYK QAGHPLIVLA GKEYGAGSSR 

       790        800        810        820        830        840 
DWAAKGPFLL GVKAVLAESY ERIHRSNLVG MGVIPLQYLP GEDARTLGLT GRERYTIIIP 

       850        860        870        880 
ENLKPQMNIQ IKLDTGKTFH AIMRFDTDVE LTYFHNGGIL NYMIRKMAS 

« Hide

References

[1]"Identification and localization of two genes on the chicken Z chromosome: implication of evolutionary conservation of the Z chromosome among avian species."
Saitoh Y., Ogawa A., Hori T., Kunita R., Mizuno S.
Chromosome Res. 1:239-251(1993) [PubMed: 8156162] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.

Cross-references

Sequence databases

D16150 mRNA. Translation: BAA03715.1.
IPIIPI00573699.
RefSeqNP_001025707.1.
UniGeneGga.4139

3D structure databases

SMRQ90875. Positions 2-888.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ90875.

Proteomic databases

PRIDEQ90875.

Genome annotation databases

EnsemblENSGALT00000003386; ENSGALP00000003381; ENSGALG00000002162; Gallus gallus. [Genome view]
GeneID373916.
KEGGgga:373916.

Organism-specific databases

CTD373916.

Phylogenomic databases

HOVERGENQ90875.

Enzyme and pathway databases

BRENDA4.2.1.3. 4.

Family and domain databases

InterProIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015937. Aconitase-like_core.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR006249. Aconitase/Fe_reg_prot_2.
IPR015934. Aconitase/Fe_reg_prot_2/AcnD.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
Gene3DG3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits.
G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit.
G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
PANTHERPTHR11670. Aconitase-like_core. 1 hit.
PTHR11670:SF1. Aconitase/Fe_reg_prot_2/AcnD. 1 hit.
PfamPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
ProDomPD000511. Aconitase_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01341. aconitase_1. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACOC_CHICK
AccessionPrimary (citable) accession number: Q90875
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 1, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents