ID A0A0V0WRI6_9BILA Unreviewed; 684 AA.
AC A0A0V0WRI6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN Name=AcCoAS {ECO:0000313|EMBL:KRX78374.1};
GN ORFNames=T06_5085 {ECO:0000313|EMBL:KRX78374.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX78374.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX78374.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX78374.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361147};
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:KRX78374.1}.
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DR EMBL; JYDK01000067; KRX78374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WRI6; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
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:SF244; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361147};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 155..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..100
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 107..502
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 565..643
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 684 AA; 76803 MW; 7BB2297AF32E8893 CRC64;
MSDNVRMATF SIAYEEDEQA ILPPPHLSEK AHCSSFSNYL EMYSQSVKDP EAFWTSFANE
LTFFKKWEKG CFLDYNFDRR KGPVYVRWMP NASLNVCYNC LDRNISRQLG DKVAFYWEGN
EPGVSMKLTY RELLKLVCKF ANVLKRKGVK KGDRVIIYMP MILELPIAML ACARIGAVHS
TVFGGYSAQA LAQRIVDAKA EVVITADGSY RGKKPILLKQ ITDQAISICE KRNVIVKHRI
IVRHLADNYT GFPSTQQDCK SKLQVQNCWF DEEMSAADEN CESEWMDSED PLFILYTSGS
TGVPKGLVHT QAGYLLYVYT TFRYVFDYQD DDVYFCTADI GWITGHSYVV YGPLANGSTV
VMFEGVPYYP EPSRYWDVVD KYGVSKFYTA PTAIRHLMKF GSSYVERCRL DRLEVLGSVG
EPINPEVWQW YYKVVGKSRC AIVDTYWQTE TGGHVLTPLP GCTNMKPGSA SFPFFGVKPV
LLNHDGQEIV GPGEGQLAFS APWPGIARSL YGNHDRYMDT YFSVPGYFST GDGKCCTRDE
DGYYWITGRI DDMMNVSGHL LSSAEIENAV VSHPAVAEAA VVCAPDPVKG QIPYCFVTLK
KDYAFTAELV LDIKQTVRNQ IGPVATPEVF QQAESLPKTR SGKILRRVLR DVAGGNTTSF
GDLSTLSEEH VIADLVNSRS SGIR
//
