ACBG1_BOVIN
ID ACBG1_BOVIN Reviewed; 726 AA.
AC Q2KHW5; Q58CT3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) 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=AAX46711.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BT021864; AAX46711.1; ALT_FRAME; mRNA.
DR EMBL; BC112858; AAI12859.1; -; mRNA.
DR RefSeq; NP_001019719.1; NM_001024548.1.
DR AlphaFoldDB; Q2KHW5; -.
DR SMR; Q2KHW5; -.
DR STRING; 9913.ENSBTAP00000043854; -.
DR PaxDb; Q2KHW5; -.
DR PRIDE; Q2KHW5; -.
DR GeneID; 515577; -.
DR KEGG; bta:515577; -.
DR CTD; 23205; -.
DR eggNOG; KOG1256; Eukaryota.
DR HOGENOM; CLU_000022_45_5_1; -.
DR InParanoid; Q2KHW5; -.
DR OrthoDB; 806831at2759; -.
DR TreeFam; TF354286; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; ISS:UniProtKB.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
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..726
FT /note="Long-chain-fatty-acid--CoA ligase ACSBG1"
FT /id="PRO_0000315807"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924N5"
FT MOD_RES 641
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99PU5"
SQ SEQUENCE 726 AA; 80585 MW; 22EC0E08E143FB72 CRC64;
MPDSRAAPQE SLLDASLGTT QENVGTSSLT DGQTLSKEPL SHALKLSTPE KVKDAQLNPP
EEALWTTRAD GRVRLRIDPI CSQTPRTVHQ MFSTTLDKYG DLSAMGFKRQ GTWEHISYTQ
YYLLARKAAK GFLKLGLERA HSVAILAFNS PEWFFSAVGA VFGGGIITGI YTTSSPEACQ
YIAYDCRANI IVVDTQKQLE KILKIWKHLP HLKAVVIYRE APPMRMPSVY TMEELMELGN
EVPEEALDVI INAQKPNQCC ALVYTSGTTG NPKGVMLSQD NITWTARYGS QAGDIQPAEI
QQEVVVSYLP LSHIAAQIYD LWTGIQWGAQ VCFAEPDALK GSLVNTLREV EPTSHMGVPR
VWEKIMEQIQ EVAAQSGFIW RKMLLWAMSV TLEQNLTCPS SDLKPFTTRL ADYLVLAKVR
QALGFAKCQK NFYGAAPMTA ETQHFFLGLN IRLYAGYGLS ETSGPHFMSS PYNYRLYSSG
KVVPGCQVKL VNEDAEGIGE ICLWGRTIFM GYLNMEDKTC EAIDAEGWLH TGDTGRLDAD
GFLYITGRLK ELIITAGGEN VPPVPIEEAV KTELPIIRNA MLIGDQRKFL SMLLTLKCTL
DPDTFEPTDN LTEQAVEFCQ RVGSKATTVS EVVGKKDEAV YQAIEEGIQR VNMNAAARPY
HIQKWAILEK DFSISGGELG PTMKLKRLAV LEKYKDVIDS FYQEQKSKQG SSLPGFSLRW
QTGASS
