ID V8NKI0_OPHHA Unreviewed; 670 AA.
AC V8NKI0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
DE Flags: Fragment;
GN Name=ACSBG2 {ECO:0000313|EMBL:ETE62799.1};
GN ORFNames=L345_11440 {ECO:0000313|EMBL:ETE62799.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE62799.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE62799.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE62799.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE62799.1}.
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DR EMBL; AZIM01003055; ETE62799.1; -; Genomic_DNA.
DR AlphaFoldDB; V8NKI0; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; 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, ECO:0000313|EMBL:ETE62799.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936}.
FT DOMAIN 209..469
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT REGION 163..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE62799.1"
SQ SEQUENCE 670 AA; 73731 MW; 65CEBA6911D78441 CRC64;
MSKGKGPAPG AGGLWTTKRD GEVKLRMDES GIDSKTPITI HDLFLATVEK YGHLPALASK
KQGQWSKLTF CQYYEECRKT AKSFLKVSGR GWAWSGSTAF ASWASTPWSG SWRTSAPFLL
GKTTTHTPAS PRGKERGVPT WRDGRRLRCR RGFEPSRFFL REGFPARPQP SKGSPPLQGA
PSLELERAPG TLRWNEFMEL GSSVPDEQLD KVLASLKPNQ CCTIIYTSGT TGNPKGITWT
ARAAGDYVHL KTALEGQESV ISYLPLSHVA AQMIDIWLPV TFGVETYFAQ PDALKGSLVD
TLREVRPTAF MGVPRVWEKM QERMKSVGAK SSTLRKKIAV WAKAVGLETN LKRMNGSIEL
PMNYRLARAL VYRKVRKALG LDRCTKCYTG AAPIMKDTLD VETLLCFAAM GSPRVGHARQ
PLTLCLTPFP SPSSCGKEIT GCQTMFFKPD QEGVGEVCFA GRHVFMGYLN MEDKTKEAID
SEGWLHSGDL GRQDEDGFLY ITGRIKELII TAGGENIPPI PIEDAIKEAV PILSNVMLVG
DKAKYLVMLM TLKSKMNLET GVSEDELTPE AVQFCQKLGS KSTKVSDIVG NKDLAVYTAI
QKGVMKVNDQ ATSNAQKIQK WLLLNRDFTI QNGELGDLRK VASVRWGNPN EAPSSGLSSV
RAASTWGEGW
//
