ID G1P6T6_MYOLU Unreviewed; 702 AA.
AC G1P6T6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000005793.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000005793.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000005793.2}
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; AAPE02024883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1P6T6; -.
DR STRING; 59463.ENSMLUP00000005793; -.
DR Ensembl; ENSMLUT00000006342.2; ENSMLUP00000005793.2; ENSMLUG00000006341.2.
DR eggNOG; KOG1256; Eukaryota.
DR GeneTree; ENSGT00940000154508; -.
DR HOGENOM; CLU_000022_45_4_1; -.
DR InParanoid; G1P6T6; -.
DR OMA; IMARTTY; -.
DR TreeFam; TF313877; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU369030};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074}.
FT DOMAIN 117..524
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 702 AA; 78140 MW; 8AEBA2FDAD5585D8 CRC64;
MMQAHELFRY FRMPELADFR QYVRTLPTNT LMGFGAFAAL TTFWYATRPR ALKPPCDLSM
QSVEVAGSDG ARRSTLLDSD EPMAYFYDDV RTVYEGFQRG IQVSNNGPCL GSRKPDQPYE
WLSYKQVEEM SECVGSALIQ KGFKAAPDQY IGIFAQNRPE WVIIEQGCFA FSMVVVPLYD
TLGTEAITYI VNKAELSLVF VDKPEKANLL LEGVENKLTP GLKVVVLMDS YGSELVERGK
KCGVEITSMK AMEDLGRANR KKPKPPAPED LAVICFTSGT TGNPKGAMIT HRNIVSDASG
FVKVTENIVN PTPDDTLISF LPLAHMFERV VECVMLCHGA KIGFFQGDIR LLMDDLKVLQ
PTIFPVVPRL LNRMFSQIFG QANTTLKRWL LDFASKRKEA ELRSCIIRNN SLWDKLIFRK
IQSNLGGKVR LMITGAAPVS ATVLTFLRAA LGCQFYEGYG QTECTAGCSL TIPGDWTAAH
AGHVGAPMPC NLIKLVDVEE MNYLAAKGEG EVCVKGPNVF QGYLKDPAKT AEALDKDGWL
HTGDIGKWLP NGALKIIDRK KHIFKLAQGE YIAPEKIENI YLRSEPVAQV FVHGESLQAF
LVAIVVPDVE TLGRWAGKRG LAGSFEELCR SKEVKKAILE DLVRLGKESG LKPFEQVKGL
ALHPELFSIE NGLLTPTMKA KRPELRNYFR SQIDELYSTI KV
//
