Human Metabolome Database: Showing Protein Peroxisomal acyl-coenzyme A oxidase 3 (HMDBP00192)

Identification Biological properties Gene properties Protein properties External links References XML Show 48 metabolites

Identification

HMDB Protein ID

HMDBP00192

Secondary Accession Numbers

5424

Name

Peroxisomal acyl-coenzyme A oxidase 3

Synonyms

BRCACox
Branched-chain acyl-CoA oxidase
Pristanoyl-CoA oxidase

Gene Name

ACOX3

Protein Type

Unknown

Biological Properties

General Function

Involved in oxidoreductase activity, acting on the CH-CH group of donors

Specific Function

Oxidizes the CoA-esters of 2-methyl-branched fatty acids (By similarity).

Pathways

alpha-Linolenic acid metabolism
Biosynthesis of unsaturated fatty acids
fatty acid metabolism
peroxisomal fatty acid beta-oxidation
Peroxisome
PPAR signaling pathway

Reactions

Acyl-CoA + Oxygen → trans-2,3-dehydroacyl-CoA + Hydrogen peroxide	details
Butyryl-CoA + FAD → FADH + Crotonoyl-CoA	details
Palmityl-CoA + FAD → (2E)-Hexadecenoyl-CoA + FADH	details
Octanoyl-CoA + FAD → (2E)-Octenoyl-CoA + FADH	details
Lauroyl-CoA + FAD → (2E)-Dodecenoyl-CoA + FADH	details
Tetradecanoyl-CoA + FAD → (2E)-Tetradecenoyl-CoA + FADH	details
Hexanoyl-CoA + FAD → trans-2-Hexenoyl-CoA + FADH	details
Decanoyl-CoA (n-C10:0CoA) + FAD → (2E)-Decenoyl-CoA + FADH	details
OPC8-CoA + FAD → trans-2-Enoyl-OPC8-CoA + FADH	details
OPC6-CoA + FAD → trans-2-Enoyl-OPC6-CoA + FADH	details
OPC4-CoA + FAD → trans-2-Enoyl-OPC4-CoA + FADH	details
Tetracosahexaenoyl CoA + FAD → Trans-2-all-cis-6,9,12,15,18,21-tetracosaheptaenoyl-CoA + FADH	details
Tetracosapentaenoyl coenzyme A, n-6 + FAD → (2E,6Z,9Z,12Z,15Z,18Z)-Tetracosahexa-2,6,9,12,15,18-enoyl-CoA + FADH	details

GO Classification

Biological Process
fatty acid beta-oxidation using acyl-CoA oxidase
Cellular Component
mitochondrion
peroxisomal matrix
Component
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
microbody
peroxisome
Function
oxidoreductase activity, acting on the ch-ch group of donors
acyl-coa dehydrogenase activity
binding
catalytic activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
oxidoreductase activity, acting on the ch-ch group of donors, oxygen as acceptor
acyl-coa oxidase activity
oxidoreductase activity
fad or fadh2 binding
Molecular Function
pristanoyl-CoA oxidase activity
acyl-CoA dehydrogenase activity
flavin adenine dinucleotide binding
Process
metabolic process
fatty acid catabolic process
fatty acid beta-oxidation
cellular metabolic process
organic acid metabolic process
oxoacid metabolic process
carboxylic acid metabolic process
monocarboxylic acid metabolic process
fatty acid metabolic process
oxidation reduction

Cellular Location

Peroxisome (Potential)

Gene Properties

Chromosome Location

Locus

4p15.3

SNPs

ACOX3

Gene Sequence

>2103 bp
ATGGCATCCACTGTGGAAGGAGGCGACACAGCTCTGCTCCCAGAATTCCCCAGGGGGCCC
CTCGATGCCTACCGAGCAAGAGCGTCCTTCAGCTGGAAGGACGTGGCGCTGTTCACGGAA
GGGGAGGGCAATGTCCGCTTTAAGAAAACCATCTTCTCAGCTCTTGAGAATGACCCTCTT
TTCGCTCGTTCCCCTGGAGCCGACCTGTCCTTGGAGAAGTATCGCGAGCTGAACTTCCTT
CGATGCAAGCGGATCTTCGAGTATGACTTCCTCAGTGTCGAAGCAATGTTCAAGAGCCCT
CTGAAGGTCCCCGCCTTGATTCAGTGCCTGGGCATGTATGACTCTTCTCTGGCTGCCAAG
TACCTCCTCCATAGCTTGGTTTTTGGATCAGCAGTTTACAGTTCTGGTTCTGAAAGACAT
CTCACATATATTCAAAAGATCTTCAGGATGGAGATTTTTGGATGTTTTGCTCTGACCGAA
TTAAGCCACGGCAGTAATACCAAGGCCATTCGCACAACTGCCCACTACGATCCTGCCACT
GAGGAATTCATCATACATTCCCCTGATTTCGAAGCTGCCAAGTTTTGGGTTGGCAACATG
GGCAAGACAGCCACTCACGCGGTGGTGTTTGCTAAGCTGTGTGTGCCAGGGGACCAGTGC
CATGGGCTGCATCCCTTTATCGTGCAGATCCGGGACCCGAAGACCCTTCTTCCCATGCCT
GGAGTGATGGTTGGCGACATAGGAAAAAAACTCGGGCAGAACGGTCTAGATAATGGTTTC
GCCATGTTCCACAAGGTCAGAGTTCCTCGCCAGAGCCTTCTGAACCGGATGGGAGACGTC
ACCCCCGAGGGCACCTATGTCAGCCCCTTTAAGGACGTCAGGCAGCGCTTTGGAGCGTCC
CTGGGGAGCCTGTCCTCGGGCCGGGTCTCCATCGTGAGCCTGGCCATCCTTAACCTAAAG
CTGGCCGTGGCCATCGCTCTTCGCTTCTCAGCCACTCGGCGTCAGTTTGGACCCACAGAG
GAGGAGGAAATACCAGTGCTTGAGTATCCAATGCAGCAATGGCGCTTGCTTCCATATCTG
GCAGCTGTCTACGGCTTAGACCATTTCTCCAAGTCGCTCTTCCTGGACCTGGTGGAGCTC
CAGCGAGGACTTGCATCGGGAGACCGCAGCGCCAGACAGGCAGAGCTTGGACGTGAGATC
CACGCCCTGGCATCGGCCAGCAAGCCCCTGGCCTCGTGGACCACCCAGCAAGGAATTCAG
GAATGCCGGGAGGCGTGTGGAGGACACGGCTATCTGGCCATGAACCGGTTGGGTGTCCTT
AGAGATGACAACGATCCCAACTGCACATACGAAGGTGACAACAACATCCTGCTGCAGCAG
ACAAGCAACTATTTGCTGGGTCTCCTGGCACACCAGGTCCACGATGGAGCTTGCTTCCGC
AGTCCGCTGAAGTCAGTGGACTTTCTGGACGCCTATCCCGGCATCCTTGACCAGAAGTTT
GAGGTCTCCAGTGTTGCCGACTGCTTGGACTCTGCAGTCGCCCTGGCAGCATACAAGTGG
CTGGTTTGCTACCTGCTCCGAGAGACTTATCAAAAATTAAACCAAGAGAAAAGATCAGGA
AGCAGTGACTTTGAAGCAAGGAACAAATGCCAGGTGTCCCACGGCCGTCCGTTGGCGCTG
GCCTTCGTGGAGCTCACGGTGGTCCAGAGGTTCCACGAGCACGTGCACCAGCCTTCCGTG
CCGCCCTCGCTGCGGGCCGTGCTGGGGCGGCTCAGTGCTCTGTACGCCCTGTGGTCCCTG
AAGCGCCACGCGGCCCTGCTCTACCGAGGAGGATACTTCTCCGGTGAGCAGGCGGGAGAA
GTGTTGGAGAGCGCCGTCCTGGCTTTGTGTTCCCAGCTGAAAGACGATGCAGTTGCCCTG
GTAGACGTGATCGCTCCTCCTGACTTTGTTCTGGACTCACCGATTGGCAGAGCCGACGGC
GAGCTCTACAAAAACCTCTGGGGCGCTGTCCTGCAGGAAAGCAAGGTGTTGGAGCGGGCA
TCCTGGTGGCCAGAGTTTTCTGTGAACAAACCTGTCATAGGAAGTCTGAAATCGAAGCTC
TAG

Protein Properties

Number of Residues

700

Molecular Weight

69574.075

Theoretical pI

8.233

Pfam Domain Function

Acyl-CoA_dh_1 (PF00441 )
Acyl-CoA_dh_M (PF02770 )
ACOX (PF01756 )

Signals

Not Available

Transmembrane Regions

Not Available

Protein Sequence

>Peroxisomal acyl-coenzyme A oxidase 3
MASTVEGGDTALLPEFPRGPLDAYRARASFSWKELALFTEGEGMLRFKKTIFSALENDPL
FARSPGADLSLEKYRELNFLRCKRIFEYDFLSVEDMFKSPLKVPALIQCLGMYDSSLAAK
YLLHSLVFGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPAT
EEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQCHGLHPFIVQIRDPKTLLPMP
GVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGAS
LGSLSSGRVSIVSLAILNLKLAVAIALRFSATRRQFGPTEEEEIPVLEYPMQQWRLLPYL
AAVYALDHFSKSLFLDLVELQRGLASGDRSARQAELGREIHALASASKPLASWTTQQGIQ
ECREACGGHGYLAMNRLGVLRDDNDPNCTYEGDNNILLQQTSNYLLGLLAHQVHDGACFR
SPLKSVDFLDAYPGILDQKFEVSSVADCLDSAVALAAYKWLVCYLLRETYQKLNQEKRSG
SSDFEARNKCQVSHGRPLALAFVELTVVQRFHEHVHQPSVPPSLRAVLGRLSALYALWSL
SRHAALLYRGGYFSGEQAGEVLESAVLALCSQLKDDAVALVDVIAPPDFVLDSPIGRADG
ELYKNLWGAVLQESKVLERASWWPEFSVNKPVIGSLKSKL

External Links

GenBank ID Protein

2326549

UniProtKB/Swiss-Prot ID

O15254

UniProtKB/Swiss-Prot Entry Name

ACOX3_HUMAN

PDB IDs

Not Available

GenBank Gene ID

GeneCard ID

GenAtlas ID

HGNC ID

References

General References

Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
Vanhooren JC, Marynen P, Mannaerts GP, Van Veldhoven PP: Evidence for the existence of a pristanoyl-CoA oxidase gene in man. Biochem J. 1997 Aug 1;325 ( Pt 3):593-9. [PubMed:9271077 ]