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   27-MAR-2024, entry version 80.
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}.
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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   AGR; Xenbase:XB-GENE-1006643; -.
DR   CTD; 379181; -.
DR   Xenbase; XB-GENE-1006643; acsbg2.L.
DR   OrthoDB; 443463at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 379181; Expressed in kidney and 19 other cell types or 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   CDD; cd05933; ACSBG_like; 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   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43272:SF101; LONG-CHAIN-FATTY-ACID--COA LIGASE ACSBG2; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 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
//