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Reviewed, UniProtKB/Swiss-Prot Q3SZP5 (ACOX1_BOVIN)

Last modified January 19, 2010. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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Names and origin

Protein namesRecommended name:
    Peroxisomal acyl-coenzyme A oxidase 1
      Short name=AOX
    EC=1.3.3.6
Alternative name(s):
    Palmitoyl-CoA oxidase
Gene names
Name: ACOX1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Catalyzes the desaturation of very long chain acyl-CoAs to 2-trans-enoyl-CoAs By similarity.

Catalytic activity

Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.

Cofactor

FAD By similarity.

Pathway

Lipid metabolism; peroxisomal fatty acid beta-oxidation.

Subcellular location

Peroxisome By similarity.

Sequence similarities

Belongs to the acyl-CoA oxidase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 660660Peroxisomal acyl-coenzyme A oxidase 1
PRO_0000281996

Regions

Motif658 – 6603Microbody targeting signal By similarity

Sites

Active site4211Proton acceptor By similarity
Binding site1391FAD By similarity
Binding site1781FAD; via amide nitrogen By similarity

Amino acid modifications

Modified residue261Phosphoserine By similarity
Modified residue2551N6-acetyllysine By similarity
Modified residue2671N6-acetyllysine By similarity
Modified residue3101Phosphoserine By similarity
Modified residue4371N6-acetyllysine By similarity
Modified residue5001N6-acetyllysine By similarity
Modified residue6431N6-acetyllysine By similarity
Modified residue6491Phosphoserine By similarity
Modified residue6511N6-acetyllysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q3SZP5-1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 606F86A63915DF9D

FASTA66074,379
        10         20         30         40         50         60 
MNPDLQKERA GASFNPELLT NVLDGSPENT RRRREIENLI LNDPDFQHEN LNFLSRSQRY 

        70         80         90        100        110        120 
EVAVKKSAIM VQKMRKFGIA DPAEIMWFKK LHLVNFVEPV GLNYSMFIPT LLNQGTTAQQ 

       130        140        150        160        170        180 
EKWLHSSKGL EIIGTYAQTE MGHGTHLRGL ETTATYDPET QEFILNSPTV TSIKWWPGGL 

       190        200        210        220        230        240 
GKTSNHAIVL AQLFTQGKCY GLHAFIVPIR ELGTHKPLPG ITVGDIGPKF GYDEMDNGYL 

       250        260        270        280        290        300 
KMDNYRIPRE NMLMKHAQVK PDGTYVKPLN NKLTYGTMVF IRSFLVGESA RSLSKACTIA 

       310        320        330        340        350        360 
VRYSAVRHQS EINPGEPEPQ ILDYQTQQYK LFPLLATAYA FQFVGAYMKE TYLRINEDIG 

       370        380        390        400        410        420 
HGDLSELPEL HALTAGLKAF TSWTTNTAIE ACRMACGGHG YSHCSGLPNI YVTFTPTCTF 

       430        440        450        460        470        480 
EGENTVMMLQ TARFLMKSYD QVHSGKLVCG MVSYLNDLPS QRIQPQQVAV WPTMVDINSP 

       490        500        510        520        530        540 
DSLTEAYKLR AARLVEIAAK NLQTEVIHRK SKEVAWNLTS IDLVRASEAH CHYVVVKLFT 

       550        560        570        580        590        600 
EKVLQIQEKS IQAVLRRLCL LYSLYGISQN AGDFLQGSIM TESQITQVNG RIKELLTAIR 

       610        620        630        640        650        660 
PDAVALVDAF DFQDVTLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY KHLKSLQSKL

« Hide

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References

[1]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.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC102761 mRNA. Translation: AAI02762.1.
IPIIPI00693965.
RefSeqNP_001030366.1.
UniGeneBt.23818

3D structure databases

HSSPHSSP built from PDB template 2DDH based on UniProtKB P07872.
SMRQ3SZP5. Positions 1-654.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3SZP5.

Genome annotation databases

EnsemblENSBTAT00000029362; ENSBTAP00000029362; ENSBTAG00000030174; Bos taurus. [Genome view]
GeneID513996.
KEGGbta:513996.

Organism-specific databases

CTD513996.

Phylogenomic databases

eggNOGmaNOG04934.
HOVERGENQ3SZP5.
InParanoidQ3SZP5.
PhylomeDBQ3SZP5.

Enzyme and pathway databases

BRENDA1.3.3.6. 251.

Family and domain databases

InterProIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR012258. Acyl-CoA_oxidase.
IPR002655. Acyl-CoA_oxidase_C.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[Graphical view]
Gene3DG3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 2 hits.
PANTHERPTHR10909:SF11. Acyl-CoA_oxidase. 1 hit.
PfamPF01756. ACOX. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
[Graphical view]
PIRSFPIRSF000168. Acyl-CoA_oxidase. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameACOX1_BOVIN
AccessionPrimary (citable) accession number: Q3SZP5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 11, 2005
Last modified: January 19, 2010
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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