ID G1PPJ5_MYOLU Unreviewed; 661 AA.
AC G1PPJ5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase ACSBG2 {ECO:0000256|ARBA:ARBA00040479};
DE EC=6.2.1.15 {ECO:0000256|ARBA:ARBA00026113};
DE EC=6.2.1.3 {ECO:0000256|ARBA:ARBA00026121};
DE AltName: Full=Acyl-CoA synthetase bubblegum family member 2 {ECO:0000256|ARBA:ARBA00043192};
DE AltName: Full=Arachidonate--CoA ligase ACSBG2 {ECO:0000256|ARBA:ARBA00042118};
GN Name=ACSBG2 {ECO:0000313|Ensembl:ENSMLUP00000012933.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000012933.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000012933.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000012933.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00024548};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000256|ARBA:ARBA00024548};
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:0000256|ARBA:ARBA00036043};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000256|ARBA:ARBA00036043};
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:0000256|ARBA:ARBA00035848};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33652;
CC Evidence={ECO:0000256|ARBA:ARBA00035848};
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:0000256|ARBA:ARBA00024497};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000256|ARBA:ARBA00024497};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC Bubblegum subfamily. {ECO:0000256|ARBA:ARBA00038034}.
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DR EMBL; AAPE02042038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02042039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02042040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02042041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PPJ5; -.
DR STRING; 59463.ENSMLUP00000012933; -.
DR Ensembl; ENSMLUT00000014221.2; ENSMLUP00000012933.2; ENSMLUG00000014216.2.
DR eggNOG; KOG1256; Eukaryota.
DR GeneTree; ENSGT00940000155332; -.
DR HOGENOM; CLU_000022_45_5_1; -.
DR InParanoid; G1PPJ5; -.
DR OMA; FNRPGPN; -.
DR TreeFam; TF354286; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IEA:Ensembl.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
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 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074}.
FT DOMAIN 50..472
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 661 AA; 73154 MW; C9F517E9F13BADA0 CRC64;
EEKAQDLEAD MTKTKASPGL WTTRPDGEVV LRMSKHGPGH EPPVTIPEYF RESVNRFGTY
SALASKNCGK WEVLTYNHYF EACRKAAKAL LKLGLERFHG VGILGFNSAE WVIASVGTIL
AGGLCVGIYA TNSADACQYV IAQAKVNVLL VENDLQLQKI LSIPQNKMGN LKAIVQYKMP
MSESNKSNLY SWDDFMELGN TIPDPQLDHI IASQKANQCA VLIYTSGTTG NPKGVMLSHD
NITWLAGTVA KDLKLACASE KQEVVVSYLP LSHIAALMMD IWLPMKVGGC TYFAQPDALK
GTLVNTLQEV KPTAFLGVPR VWEKIQAKIK ESCAKSSSLK NKVFAWARTV GLKVNTKRMQ
GIHDAPMSYH VAKALVFNKR NSIGFDHCHL FISGAPLSPE TAEFFLSLDI PIGEMYGMSE
SSGPHTVSNF DNLRMLSCGK IASGCKNMLL QPTSDGIGEV CMWGRHVFMG YLEKQEETME
IIDEEGWLHS GDLGLMDNQG FLYITGRIKE MLITAGGENV APVPIENRVK EKIPIVSNAL
LVGDKAKFLS ILLTLKKKKK KLEGPWKKMN WEATKFCQDL GSQASTVSEI VELQDALVYS
AIQKGIDDVN QEAISNAQKI QKWVILEKDF SIYGGELGPT AKMKRNSITQ KYRKQIENLY
H
//
