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Information on EC 7.6.2.4 - ABC-type fatty-acyl-CoA transporter

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EC Tree
IUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes. In humans, it is associated with Zellweger's syndrome.
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UNIPROT: P34230
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
fatty acyl CoA[side 1]
=
+
+
fatty acyl CoA[side 2]
Synonyms
comatose, abcd1, abcd2, pmp70, abcd3, adrenoleukodystrophy protein, aldrp, pat1p, 70-kda peroxisomal membrane protein, peroxisomal abc transporter, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
fatty-acyl-CoA-transporting ATPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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transmembrane transport
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, fatty-acyl-CoA-transporting)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes. In humans, it is associated with Zellweger's syndrome.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform Pxa2
UniProt
Manually annotated by BRENDA team
isoform Pxa2
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
very long chain acyl-CoA esters are hydrolyzed by the Pxa1p-Pxa2p complex prior to the actual transport of their fatty acid moiety into the peroxisomes with the CoA presumably being released into the cytoplasm. The Pxa1p-Pxa2p complex functionally interacts with the acyl-CoA synthetases Faa2p and/or Fat1p on the inner surface of the peroxisomal membrane for subsequent re-esterification of the very long chain fatty acids
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PXA2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
853
0
97126
Swiss-Prot
other Location (Reliability: 1)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
van Roermund, C.W.; Ijlst, L.; Majczak, W.; Waterham, H.R.; Folkerts, H.; Wanders, R.J.; Hellingwerf, K.J.
Peroxisomal fatty acid uptake mechanism in Saccharomyces cerevisiae
J. Biol. Chem.
287
20144-20153
2012
Saccharomyces cerevisiae (P34230), Saccharomyces cerevisiae (P41909), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (P34230), Saccharomyces cerevisiae ATCC 204508 (P41909)
Manually annotated by BRENDA team