ACBG2_XENLA
ID ACBG2_XENLA Reviewed; 739 AA.
AC Q7ZYC4; Q2TAG2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase ACSBG2 {ECO:0000250|UniProtKB:Q5FVE4};
DE EC=6.2.1.3 {ECO:0000250|UniProtKB:Q5FVE4};
DE AltName: Full=Acyl-CoA synthetase bubblegum family member 2;
DE AltName: Full=Arachidonate--CoA ligase ACSBG2 {ECO:0000250|UniProtKB:Q5FVE4};
DE EC=6.2.1.15 {ECO:0000250|UniProtKB:Q5FVE4};
GN Name=acsbg2 {ECO:0000250|UniProtKB:Q5FVE4};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of fatty acids such as long chain
CC and very long-chain fatty acids to their active form acyl-CoAs for both
CC synthesis of cellular lipids, and degradation via beta-oxidation. Can
CC activate diverse saturated, monosaturated and polyunsaturated fatty
CC acids. {ECO:0000250|UniProtKB:Q5FVE4}.
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:0000250|UniProtKB:Q5FVE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
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:0000250|UniProtKB:Q5FVE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
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:0000250|UniProtKB:Q5FVE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-
CC octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33652;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate +
CC tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000250|UniProtKB:Q5FVE4};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC Bubblegum subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC043850; AAH43850.1; -; mRNA.
DR EMBL; BC110943; AAI10944.1; -; mRNA.
DR RefSeq; NP_001079494.1; NM_001086025.1.
DR AlphaFoldDB; Q7ZYC4; -.
DR SMR; Q7ZYC4; -.
DR DNASU; 379181; -.
DR GeneID; 379181; -.
DR KEGG; xla:379181; -.
DR CTD; 379181; -.
DR Xenbase; XB-GENE-1006643; acsbg2.L.
DR OrthoDB; 806831at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 379181; Expressed in kidney and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; ISS:UniProtKB.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..739
FT /note="Long-chain-fatty-acid--CoA ligase ACSBG2"
FT /id="PRO_0000315816"
FT BINDING 287..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 478..483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 556
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 45
FT /note="P -> S (in Ref. 1; AAI10944)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="E -> D (in Ref. 1; AAI10944)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="H -> Q (in Ref. 1; AAI10944)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="Missing (in Ref. 1; AAI10944)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 739 AA; 81620 MW; 2FF24B6619F52A97 CRC64;
MAAVISNSSG TELYVDPTKA IPDLCINDVV LSTPPCYAEE TLVQPSAEIN TSNSSEKPIV
PEISSSDVMV HSAVENLPTS DMKLWTAQRD SAVKLRLEDS DVASLPPVTI HQLFQETVNK
YGDYVALASK QGDQWHKMSY KQYYEQCRIA AKGFIKLGLE RYHGVGILGF NSAEWFIADV
GAIFAGGFAV GIYTTNSAEA CHYVAQNCEA NIIVVENQKQ LQKILQVQDQ LPHLKAIIQY
KDELKEKRPN LYTWKEFMQL GKDIPDSQLD QIISSQKPNQ CCTLIYTSGT TGQPKGVMLS
HDNITWTAAA AGKTVRLREA TDLQEIVVSY LPLSHIAAQM IDIWLTMKYG GATYFAQPDA
LKGSLAITLR EVRPTAFMGV PRVWEKMQEK MKAVGAKSST IKRKMATWAK GVGLETNLKK
MNGSTPHPMK YHVANKLVFK KVRKALGLDR CTKCYTGAAP ITKDTLEFFL SLNIPVYELY
GMSESSGPHT ISLPDAFRIT SCGKVISGCK TKIHQPDSDG SGEILFWGRH VFMGYLNMED
KTHESLDEEG WLHSGDIGKH DENGFLYITG RIKELIITAG GENIPPVPTE DAVKEQVPII
SNAMLIGDKK KFLSMLLTLK CNVNADTGEP EDELTPEAIQ FCRQIGSKAT LVSDIVGGKD
TAVYAAIQEG VNSVNEKSTS NAQKVQKWLI LEKDFSITGG ELGPTMKLKR PVVAKMYKDQ
IDSFYQDAGT PTENFTPPK
