ID V8PA91_OPHHA Unreviewed; 685 AA.
AC V8PA91;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN Name=ACSS2 {ECO:0000313|EMBL:ETE71250.1};
GN ORFNames=L345_02930 {ECO:0000313|EMBL:ETE71250.1};
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:ETE71250.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE71250.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE71250.1};
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=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA;
CC Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:456215; EC=6.2.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000787};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC Evidence={ECO:0000256|ARBA:ARBA00000787};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456215; EC=6.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001884};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177;
CC Evidence={ECO:0000256|ARBA:ARBA00001884};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU361147}.
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:ETE71250.1}.
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DR EMBL; AZIM01000400; ETE71250.1; -; Genomic_DNA.
DR AlphaFoldDB; V8PA91; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd05966; ACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF126; ACETYL-COENZYME A SYNTHETASE, CYTOPLASMIC; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361147};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU361147};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361147};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936}.
FT DOMAIN 31..91
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 100..512
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 567..645
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 685 AA; 77814 MW; F678905B850EB382 CRC64;
MVLPKAEHAA RLYRAPPELA REAHVSSLEK YRELYRRSVE EPQEFWGEIA KQFYWRNQHT
GPFLQYNFDV TKGKIFIEWM KGATTNICYN VLDRNVYENK LGDKIAFYWE GNEPGDSMKI
TYSELLSKVC QFANVLREQG IKKGDRVSIY MPMIIELVVA MLACARIGAL HSIVFAGFSA
ESLCERILDS NCSLLITADA FYRGDKLINL KQIADEALQK CKAKSNPLER CIVVKHLGRE
ELVQDGTSSK SPPLKRICQS VQTPWDPEVD LWWHDIMKNA SKECEPVWCD AEDELFILYT
SGSTGKPKGV VHTIAGYMLF TAATFKYVFD HHPEDIYWCT ADIGWITGHS YLTYGPLANG
ATSVLFEGLP IYPDVSRMWN IIDKYKVTKF YTAPTAIRLL MKYGDEPVKK YSRKSLKVLG
TVGEPINPEA WLWFYRVVGE ERCPIVDTFW QTETGGHVLT PLPYATPMKP GSATFPFFGV
VPAVLDESGE ELEGEAEGYL VFKQPWPGIM RTVYKNQQRF EATYFQKFPG YYVTGDGCKR
DKDGYYWITG RIDDMLNVSG HLLSTAEVES ALVEHASISE AAVVSHPHPV KGECLYCFVT
LKDGHDFTSK LIDELRKQVR EKIGPIATPD YIQNAPSLPK TRSGKIMRRV LRKIAKNDRE
LGDTSTVADP AVINHLFSNR CETIM
//
