ID   ACBG2_CHICK             Reviewed;         763 AA.
AC   Q5ZKR7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   24-JAN-2024, entry version 98.
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}; ORFNames=RCJMB04_9i11;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Mediates activation of long-chain fatty acids for both
CC       synthesis of cellular lipids, and degradation via beta-oxidation.
CC       {ECO:0000250}.
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAG31676.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ720017; CAG31676.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q5ZKR7; -.
DR   SMR; Q5ZKR7; -.
DR   STRING; 9031.ENSGALP00000045078; -.
DR   PaxDb; 9031-ENSGALP00000040940; -.
DR   VEuPathDB; HostDB:geneid_420090; -.
DR   eggNOG; KOG1256; Eukaryota.
DR   InParanoid; Q5ZKR7; -.
DR   PhylomeDB; Q5ZKR7; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
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..763
FT                   /note="Long-chain-fatty-acid--CoA ligase ACSBG2"
FT                   /id="PRO_0000315815"
FT   REGION          47..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         281..289
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         472..477
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         550
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         565
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         678
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   763 AA;  84207 MW;  01B065BA33BCAB43 CRC64;
     MLCESEARST LADPVPMAYL SVDAQGSSEV SLDDITINSS AGTVEVCSMK PADDPKTERS
     QMNKTGLASS SRPASNVWTT QQDGEVKLRM DEEGMGSEAP KTVHEVFQEA VSKYGDYYAL
     ASKKNGQWVK LTYKMYYDKC WKAAKSFLKL VLERFHGVCI LGFNSPEWFI ADIGAIFAGG
     LAVGIYTTNS PEACHYVAEN CSANILVVEN HTQACRKSLE IEHKLPHMKA IIQYGEELKE
     KRPNQYSWRE FLDLGEDIPD SQLREIIESQ KPNQCCTLIY TSGTTGQPKG VMLSHDNLTW
     TSIAAGRSLM LLEATEKQEL VVSYLPLSHV AAQMIDIWLP VTFGGQVFFA QPDALKGTLV
     DTLREVRPTA FLGVPRVWEK IEEKMKSVGA KSSTLRRKVA SWAKGVGLQT NLKWMNGHSE
     VPMNFRLARQ LVYKKVRKAI GLDRCTKCFT GAAPISRETL EFFLSLNIPV FELYGMSESS
     GPHTVSIPQA FRLTSCGKEM AGCRTLIHKP DADGIGEICF AGRHIFMGYL NMEEKTKEAI
     DKDGWLHSGD LGKCDKDGFI YITGRIKELI ITAGGENVPP VPIEDAVKEA CPIISNAMLV
     GDKAKFLAML LTLKCIINTE SGEPGDDLTA EAIEYCQKLG SKATKVSEII SSKDKAVYAA
     IQAAVSEVNK RAVSNAQKIQ KWVVLEKDFS VGGGELGPTM KLKRPVVAQK YKDLIDEFYA
     DANTPTTTEE RTSAVMWGGR KLPLVHSIVS LGSLQQIQRV LQK
//