ID H2TTH6_TAKRU Unreviewed; 677 AA.
AC H2TTH6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN Name=LOC101068854 {ECO:0000313|Ensembl:ENSTRUP00000027984.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000027984.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000027984.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000027984.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; H2TTH6; -.
DR STRING; 31033.ENSTRUP00000027984; -.
DR Ensembl; ENSTRUT00000028094.3; ENSTRUP00000027984.3; ENSTRUG00000011086.3.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000165253; -.
DR InParanoid; H2TTH6; -.
DR OMA; TVHTKKI; -.
DR OrthoDB; 144557at2759; -.
DR TreeFam; TF354241; -.
DR Proteomes; UP000005226; Chromosome 16.
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:SF83; ACETYL-COENZYME A SYNTHETASE; 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:UP000005226}.
FT DOMAIN 50..103
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 105..495
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 553..632
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 677 AA; 75066 MW; 20F06D5913CF8F69 CRC64;
MLPCAERVVA SISRRLFRSY LSVSSRRRCN ITAFMPEAAG FDGVSDRSTL QDFSVSNSEK
FWAAAARHRL SWIRTFDAVR DCDLSRGKIK WFEGGKLNVS VNCLDRHVHT CPDKVALIWE
RDEPGSEVKV TYRELLDMTC RLGNLLRRRG VKRGDCVTIY MPPCPMAVAS MLACARIGAA
HNVVFAGFSA EALSERIRDA QSSTVITVNQ GVRGGKLVEL KKTVDEAVQS CPTVQQVFVA
TRTENPVLMA ARDVALDEEM LKEDVVCEPE AMDSEDVLFL LYTSGSTGKP KGLVHTQAGY
LLYAALTHRY VFSYQDGDVF GCVADIGWIT GHSYTVYGPL ANGGTTVLFE STPIYPDPGR
YWEMVQRLKI NQFYGAPTAI RLLLKYGDQW VRKYDRSTLK TLGSVGEPIN TEAWEWYHTV
VGDGRCPVVD TWWQTETGGI CISPKPSDPD AEIIPGMAMR PFFGIKPVLM DTEGNVQSSS
DTSGALCIAQ PWPGMARTIH NNHQRFIETY CQPHPGYFFT GDGAYCSKEG YYQITGRLDD
VINVSGHRIG TAEIEDVVNQ CPVVAESAVI GYAHDIKGEG VFAFAVLKQG VDTQYGDVSQ
QLKDTVSKKI AKYASPDHIQ FVKRLPKTRS GKIMRRVLRK IVEGDLEGLG DLSTLDDPTA
VQEIIQGNSE LCNKHKP
//
