A8K9T3 · A8K9T3_HUMAN

  • Protein
    Long-chain-fatty-acid--CoA ligase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

Function

function

Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation.

Catalytic activity

  • (5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate
    This reaction proceeds in the forward direction.
    EC:6.2.1.15 (UniProtKB | ENZYME | Rhea)
  • (E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP + diphosphate
    This reaction proceeds in the forward direction.
  • 12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + ATP + CoA = 12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate
    This reaction proceeds in the forward direction.
  • 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + ATP + CoA = 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-CoA + AMP + diphosphate
    This reaction proceeds in the forward direction.
  • 5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = 5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate
    This reaction proceeds in the forward direction.
  • ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-CoA
    This reaction proceeds in the forward direction.
  • a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
    This reaction proceeds in the forward direction.
    EC:6.2.1.3 (UniProtKB | ENZYME | Rhea)

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Cellular Componentmitochondrial outer membrane
Molecular FunctionATP binding
Molecular Functionlong-chain fatty acid-CoA ligase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Long-chain-fatty-acid--CoA ligase
  • EC number
  • Alternative names
    • Acyl-CoA synthetase
    • Long-chain acyl-CoA synthetase

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    A8K9T3

Subcellular Location

Mitochondrion outer membrane
; Single-pass membrane protein
Endoplasmic reticulum membrane
; Single-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane21-45Helical

Keywords

  • Cellular component

Disease & Variants

Organism-specific databases

PTM/Processing

Proteomic databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain116-520AMP-dependent synthetase/ligase

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    698
  • Mass (Da)
    77,952
  • Last updated
    2007-12-04 v1
  • Checksum
    C8D996C0DD8974A8
MQAHELFRYFRMPELVDFRQYVRTLPTNTLMGFGAFAALTTFWYATRPKPLKPPCDLSMQSVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGHRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK292798
EMBL· GenBank· DDBJ
BAF85487.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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