ACBG2_CHICK
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 03-AUG-2022, entry version 93.
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};
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; AJ720017; CAG31676.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q5ZKR7; -.
DR SMR; Q5ZKR7; -.
DR STRING; 9031.ENSGALP00000040940; -.
DR PaxDb; Q5ZKR7; -.
DR PRIDE; Q5ZKR7; -.
DR VEuPathDB; HostDB:geneid_420090; -.
DR eggNOG; KOG1256; Eukaryota.
DR InParanoid; Q5ZKR7; -.
DR PhylomeDB; Q5ZKR7; -.
DR Proteomes; UP000000539; Unplaced.
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 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..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
