ID A0A3Q1BH27_AMPOC Unreviewed; 698 AA.
AC A0A3Q1BH27;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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=6.2.1.3 {ECO:0000256|RuleBase:RU369030};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000012898.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000012898.1}
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000256|ARBA:ARBA00024548};
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC Evidence={ECO:0000256|ARBA:ARBA00024565};
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113;
CC Evidence={ECO:0000256|ARBA:ARBA00024495};
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117;
CC Evidence={ECO:0000256|ARBA:ARBA00024532};
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109;
CC Evidence={ECO:0000256|ARBA:ARBA00024469};
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000256|ARBA:ARBA00024497};
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 -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU369030}.
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DR STRING; 80972.ENSAOCP00000012898; -.
DR Ensembl; ENSAOCT00000020765.1; ENSAOCP00000012898.1; ENSAOCG00000017472.1.
DR Ensembl; ENSAOCT00000030812.1; ENSAOCP00000028037.1; ENSAOCG00000017472.1.
DR GeneTree; ENSGT00940000154508; -.
DR OMA; RRINHAG; -.
DR OrthoDB; 443463at2759; -.
DR Proteomes; UP000257160; Unplaced.
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};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU369030};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160}.
FT DOMAIN 116..519
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 698 AA; 77624 MW; 44D2CFCB51ECFB71 CRC64;
MLSQEFLQKL RLPDMDNVSE YVRSISTPML VSMGAVAAAT TYYLATRPKA LPPVCDLHMQ
SVEVPGGDLA RQSALQNGES HLTHIYDDAR TMYEFFLRGA RVSNNGPCLG SRKPKQPYEW
ISYREVRERT ENLGSAFLHK GHSKTTDPHI GIFSQNRPEW TISELACYTY SLVSVPLYDT
LGTDAIAYII DKASITTVVC DVTDKVNLVL DCVKDIKHSV KTIVLMETPS ADLVERGQQA
GIHILSLQEM EAIGKANHRQ PMPPRPEDMA VICFTSGTTG NPKGAMLTHG NIVSNCSAFI
KITEIFCPLG PSDVHISYLP LAHMFERVVQ GVMLVQGARI GFFQGDIRRL SDDLNTLKPT
VFPVVPRLLN RMYDKIFGQA NTSLKRWLLG FAYRRKQAEM MKGIMRRDSI WDRLIFRKVQ
ASLGGCVRLM LTGAAPISPT VLTFLRAAVG CQFYEGYGQT ECTAGCTLTM PGDWSAGHVG
APLPCNSVKL VDVPEMNYLA VNGEGEVCVK GTNVFQGYLK DPEKTAETID ADGWVHTGDI
GKWLPNGTLK IVDRKKHIFK LAQGEYIAPE KIENVYTRSD AVAQIFVHGD SLQACLVAVV
VPDPDFLSDW TKRMLGLQGS YQELCGRAEV KAAILEDMLR LGKEGGLKSF EQVKAIYIHT
KQFSIENGLL TPTMKAKRNE MRQYFRSQID ELYAGIKM
//
