[1]	NUCLEOTIDE SEQUENCE [MRNA]. Baumgart E., Van Veldhoven P.P., Althoff B., Mannaerts G.P., Voelkl A., Fahimi D.; "Molecular characterization of guinea pig peroxisomal palmitoyl-CoA oxidase 1."; Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.

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).
SIMILARITY: Belongs to the acyl-CoA oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ005112; CAA06376.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P07872; 1IS2. [HSSP ENTRY / PDB]

SMR

Q9Z1N0; 1-655.

ModBase

Q9Z1N0.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from sequence or structural similarity from UniProtKB).
GO:0003995;	Molecular function: acyl-CoA dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0003997;	Molecular function: acyl-CoA oxidase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0006635;	Biological process: fatty acid beta-oxidation (inferred from electronic annotation from InterPro).
GO:0006091;	Biological process: generation of precursor metabolites and energy (inferred from sequence or structural similarity from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006693;	Biological process: prostaglandin metabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR006091; Acyl-CoA_DHase/Oxase_M.
IPR012258; Acyl-CoA_oxidase.
IPR002655; Acyl_CoA_ox_C.
IPR013786; AcylCoA_DH/ox_N.
IPR013764; AcylCoA_oxidase/DH_1/2_C.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 2.

PANTHER

PTHR10909:SF11; Acyl-CoA_oxidase; 1.

Pfam

PF01756; ACOX; 1.
PF02770; Acyl-CoA_dh_M; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000168; Acyl-CoA_oxidase; 1.

ProtoNet

Q9Z1N0.

Phylogenomic databases

HOVERGEN

Q9Z1N0; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase; Peroxisome; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 661`	`661`	`Peroxisomal acyl-coenzyme A oxidase 1.`	`PRO_0000204676`
`MOTIF`	`659 661`	`3`	`Microbody targeting signal (By similarity).`
`MOD_RES`	`26 26`		`Phosphoserine (By similarity).`
`MOD_RES`	`267 267`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`310 310`		`Phosphoserine (By similarity).`
`MOD_RES`	`643 643`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`649 649`		`Phosphoserine (By similarity).`

Sequence information

Length: 661 AA [This is the length of the unprocessed precursor]

Molecular weight: 74390 Da [This is the MW of the unprocessed precursor]

CRC64: D360D9515259E76A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNPDLRRERA AATFNPELIT HLLDGSPEKT RRRREIENKI LSDPDFQHEN HNFLTRSERY 

        70         80         90        100        110        120 
EAAIKKSAVM VKKMREFGIA DPDEIMWFKR LLLGNFVEPV GLNYSMFIPT LLNQGTTAQQ 

       130        140        150        160        170        180 
EKWLHPSTGL QIIGTYAQTE MGHGTHLRGL ETTATYDPKT QEFIINSPTV TSIKWWPGGL 

       190        200        210        220        230        240 
GKTSNHAIVL AQLITQGKCY GLHAFIVPIR EIGTHKPLPG ITVGDIGPKF GYEEMDNGYL 

       250        260        270        280        290        300 
KMDNYRIPRE NMLMKYAQVK PDGTYVKPVS NKLTYGTMVF VRSFLVGAAA QSLSKACTIA 

       310        320        330        340        350        360 
IRYSAVRHQS EIKPGEPEPQ VLDFQTQQYK LFPILATAYA FQFVGSYMKD TYHRINESIG 

       370        380        390        400        410        420 
QGDLSELPEL HALTAGLKAF TTWTANAGIE ECRLACGGHG YSHCSGIPNI YVTFTPACTF 

       430        440        450        460        470        480 
EGENTVMMLQ TARFLMKVYD QVQSGKLVHG LVSYLNDLPS QRIQPQQVAV WPTVVDINNP 

       490        500        510        520        530        540 
DSLTEIYKLR AARLIDIAAK SLQGEMSHRK SKEVAWNLTS VGLVRATDAH CHYVVVKLFA 

       550        560        570        580        590        600 
DKLLKIQDKT IQAVLRNLFL LYSLYGISQK AGDFLQGNIM TGSQITQVNQ RVLELLAVIR 

       610        620        630        640        650        660 
PNAVALVDAF DYKDITLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY HKYLKPLQSK 


L

Q9Z1N0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools