ID A0A2Y9PSQ8_DELLE Unreviewed; 675 AA.
AC A0A2Y9PSQ8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN Name=ACSS1 {ECO:0000313|RefSeq:XP_022449884.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022449884.1};
RN [1] {ECO:0000313|RefSeq:XP_022449884.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022449884.1};
RG RefSeq;
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 RefSeq; XP_022449884.1; XM_022594176.1.
DR AlphaFoldDB; A0A2Y9PSQ8; -.
DR Ensembl; ENSDLET00000007311; ENSDLEP00000006597; ENSDLEG00000004910.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
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:SF110; ACETYL-COENZYME A SYNTHETASE 2-LIKE, MITOCHONDRIAL; 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:UP000248483}.
FT DOMAIN 44..100
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 102..488
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 550..628
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 675 AA; 73896 MW; 33548128044D645A CRC64;
MAASCLGRGV VRLLGGLRGV GARGLAAPRL WGSASAPAAP AGSYQERIAL AASEPAAFWG
PLARDVLVWD TPYHTVSDCD FRSGRIGWFL GGQLNVSVNC LDQHVRKSPE SVALIWEQDE
PGTEVRITYR ELLETTCRLA NTLKRHGVHR GDRVAIYMPV SPLAVAAMLA CARIGAIHTV
VFAGFSAGSL AARINDAKCK VVITFNQGLR GGRVVELKKI VDEAVKLCPT VQHVLVAHRT
DNKVHMGDLD IPLEQEMAKE EPVCAPESMG SEDTLFLLYT SGSTGTPKGL VHTQAGYLLY
AALTHRFVFD YRPGDVFGCV ADIGWITGHS YVVYGPLCNG ATSVLFESTP VYPDAGRYWE
MVQRLKINQF YGSPTAFRLL LKFEDSWVKK YDRSSLRTLG SVGEPINHEA WQWLHRVVGD
SRCTLVDTWW QTETGGICIS PRPSEEGAEI LPCMAMRPLF GIVPVLMDEK GNVLKGGDVS
GALCLSQAWP GMARTIFGDH QRFMDAYFEA YPGYYFTGDG AYRTEDGYYQ ITGRMDDVIN
ISGHRLGTAE IEDAMADHPA VPETAVIGYP HDIKGEAAFA FIVLKDDAGD ADVVVKELRS
VVASKIAKYA VPDQVLVVKR LPKTRSGKVM RRLLRKIVTG RAQDLGDITT MEDPTVITEI
LSAYQEYKDK SGAAQ
//
