ID A0A2I3GDG0_NOMLE Unreviewed; 683 AA.
AC A0A2I3GDG0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|RuleBase:RU369030};
DE EC=6.2.1.15 {ECO:0000256|RuleBase:RU369030};
DE EC=6.2.1.3 {ECO:0000256|RuleBase:RU369030};
DE AltName: Full=Acyl-CoA synthetase {ECO:0000256|RuleBase:RU369030};
DE AltName: Full=Long-chain acyl-CoA synthetase {ECO:0000256|RuleBase:RU369030};
GN Name=ACSL1 {ECO:0000313|Ensembl:ENSNLEP00000029351.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000029351.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000029351.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000029351.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the conversion of long-chain fatty acids to their
CC active form acyl-CoAs for both synthesis of cellular lipids, and
CC degradation via beta-oxidation. {ECO:0000256|RuleBase:RU369030}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:456215; EC=6.2.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00024548,
CC ECO:0000256|RuleBase:RU369030};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000256|ARBA:ARBA00024548,
CC ECO:0000256|RuleBase:RU369030};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP
CC + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526,
CC ChEBI:CHEBI:72745, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000256|ARBA:ARBA00024565,
CC ECO:0000256|RuleBase:RU369030};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC Evidence={ECO:0000256|ARBA:ARBA00024565,
CC ECO:0000256|RuleBase:RU369030};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + ATP + CoA = 12-
CC hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:52112, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:90718, ChEBI:CHEBI:136408,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00024495,
CC ECO:0000256|RuleBase:RU369030};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113;
CC Evidence={ECO:0000256|ARBA:ARBA00024495,
CC ECO:0000256|RuleBase:RU369030};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + ATP + CoA = 15-
CC hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:52116, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:78832, ChEBI:CHEBI:136409,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00024532,
CC ECO:0000256|RuleBase:RU369030};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117;
CC Evidence={ECO:0000256|ARBA:ARBA00024532,
CC ECO:0000256|RuleBase:RU369030};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = 5-
CC hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:52108, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:65341, ChEBI:CHEBI:136407,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00024469,
CC ECO:0000256|RuleBase:RU369030};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109;
CC Evidence={ECO:0000256|ARBA:ARBA00024469,
CC ECO:0000256|RuleBase:RU369030};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000256|ARBA:ARBA00024497,
CC ECO:0000256|RuleBase:RU369030};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000256|ARBA:ARBA00024497,
CC ECO:0000256|RuleBase:RU369030};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000256|ARBA:ARBA00024484};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000256|RuleBase:RU369030}; Single-pass membrane protein
CC {ECO:0000256|RuleBase:RU369030}. Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU369030}; Single-pass membrane protein
CC {ECO:0000256|RuleBase:RU369030}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU369030}.
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DR EMBL; ADFV01066186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01066187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01066188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01066189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3GDG0; -.
DR Ensembl; ENSNLET00000040233.1; ENSNLEP00000029351.1; ENSNLEG00000011041.3.
DR GeneTree; ENSGT00940000154508; -.
DR Proteomes; UP000001073; Chromosome 7b.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:InterPro.
DR CDD; cd05927; LC-FACS_euk; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR045311; LC-FACS_euk.
DR PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43272:SF28; LONG-CHAIN-FATTY-ACID--COA LIGASE 1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU369030};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832,
KW ECO:0000256|RuleBase:RU369030};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU369030};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU369030}; Membrane {ECO:0000256|RuleBase:RU369030};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU369030};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Transmembrane {ECO:0000256|RuleBase:RU369030};
KW Transmembrane helix {ECO:0000256|RuleBase:RU369030}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369030"
FT DOMAIN 116..505
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 683 AA; 76291 MW; 5770A5E1333B7FC3 CRC64;
MQAHELFRYF RMPELVDLRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKP LKPPCDLSMQ
SVEVAGSGGA RRSALLDSDE PLVYFYDDVT TLYEGFQRGI QVSNNGPCLG SRKPDQPYEW
LSYKQVAELS ECIGSALIQK GFKTAPDQFI GIFAQNRPEW VIIEQGCFAY SMVIVPLYDT
LGNEAITYIV NKAELSLVFV DKPEKAKLLL EGVENKLIPG LKIIVLMDAY GSELVERGQK
CGVEIISMKA MEDLGRANRR KPKPPAPEDL AVICFTSGTT GNPKGAMITH RNIVSDCSAF
VKATELCNPC CDDKMFCVML CHGAKIGFFQ GDIRLLMDDL KVLQPTIFPV VPRLLNRMFD
RIFGQANTTL KRWLLDFASK RKEAELRSGI IRNNSLWDRL IFHKVQSSLG GRVRLMVTGA
APVSATVLTF LRAALGCQFY EGYGQTECTA GCCLTMPGDW TAGHVGAPMP CSLIKLVDVE
EMNYMAAEGE GEVCVKGPNV FQGYLKDPVK TAEALDKDGW LHTGDIGKWL PNGTLKIIDR
KKHIFKLAQG EYIAPEKIEN IYVRSEPVAQ VFVHGESLQA FLIAIVVPDV ETLCSWARKR
GFEGSFEELC RNKDVKKAIL EDMVRLGKDS GLKPFEQVKG ITLHPELFSI DNGLLTPTMK
AKRPELRNYF RSQIDELYST IKV
//
