ACBG1_MACFA
ID ACBG1_MACFA Reviewed; 724 AA.
AC Q4R4P9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase ACSBG1 {ECO:0000250|UniProtKB:Q96GR2};
DE EC=6.2.1.3 {ECO:0000250|UniProtKB:Q96GR2};
DE AltName: Full=Acyl-CoA synthetase bubblegum family member 1;
GN Name=ACSBG1 {ECO:0000250|UniProtKB:Q96GR2}; ORFNames=QtrA-12214;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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:Q96GR2}.
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:Q96GR2};
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:0000250|UniProtKB:Q96GR2};
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:Q96GR2};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96GR2}.
CC Cytoplasmic vesicle {ECO:0000250}. Microsome {ECO:0000250}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:Q96GR2}. Cell membrane
CC {ECO:0000250|UniProtKB:Q96GR2}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC Bubblegum subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE01926.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB169845; BAE01926.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q4R4P9; -.
DR SMR; Q4R4P9; -.
DR STRING; 9541.XP_005560257.1; -.
DR eggNOG; KOG1256; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; 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; -; 2.
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; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Membrane; Microsome; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..724
FT /note="Long-chain-fatty-acid--CoA ligase ACSBG1"
FT /id="PRO_0000315809"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 282..290
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 701
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924N5"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PU5"
FT MOD_RES 658
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99PU5"
SQ SEQUENCE 724 AA; 80998 MW; FD4738EC60704BF3 CRC64;
MPRNSGAGYG CPHGDPSMLD SRETPQESRQ DMTVGTTQEK LKTSSLTDRQ PLSKESLNHA
LKLSVPEKVN NAQWDAPEEA LWTTRADGRV RLRIDPSCPQ LPYTVHRMFY EALDKYGDFS
ALGFKCQDKW EHISYSQYYL LARRAAKGFL KLGLERAHSV AILGFNSPEW FFSAVGTVFA
GGIVTGIYTT SSPEACQYIA YDCCANVIMV DTQKQLEKIL KVWKQLPHLK AVVIYKEPPP
NKMANVYTME EFMELGNEVP EEALDAIIDT QQPNQCCVLV YTSGTTGNPK GVMLSQDNIT
WTARYGSQAG DIRPAEVQQE VVVSYLPLSH IAAQIYDLWT GIQWGAQVCF AEPDALKGSL
VNTLREVEPT SHMGVPRVWE KIMERIQEVA AQSGFIRRKM LLWAMSVTLE QNLTCPGSDL
KPFTTRLADY LVLAKVRQAL GFAKCQKNFY GAAPMTAETQ HFFLGLNIRL YAGYGLSETS
GPHFMSSPCN YRLYSSGKLV PGCRVKLVNQ DTEGIGEICL WGRTIFMGYL NMEDKTCEAI
DEEGWLHTGD AGRLDADGFL YITGRLKELI ITAGGENVPP VPIEEAVKME LPIISNAMLI
GTDQRKFLSM LLTLKCTLDP DTSDPTDNLT EQAVEFCQRV GSRATTVSEI VGKDEAVYQA
IEEGIRRVNM NAAARPYHIQ KWAILERDFS ISGGELGPTM KLKRLTVLEK YKDIIDSFYR
EQKM
