ID A0A0N4ZIF3_PARTI Unreviewed; 682 AA.
AC A0A0N4ZIF3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000770700.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0000770700.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0N4ZIF3; -.
DR STRING; 131310.A0A0N4ZIF3; -.
DR WBParaSite; PTRK_0000770700.1; PTRK_0000770700.1; PTRK_0000770700.
DR Proteomes; UP000038045; Unplaced.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361147}.
FT DOMAIN 37..96
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 102..500
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 561..639
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 682 AA; 75131 MW; 3D41E5FB63FA18DC CRC64;
MSDCKVKFEL EGSRGSRLFQ PPSNLSASAH IKGIKSYHEK YRSSLNDSDK FWRNVASELY
FEKMTDNGLE WNFNKDKGKI FVNFMKGSKT NIAYNCLERN IARGLGDKVA FKFEGNEPGD
EDSITYKQLL EKVIAFSAVL RSKGVKKGDV VAIYLPMSFE LPIAMLACAR IGAIHSIVFA
GFSSESLANR IIHCQAKVLI TANAFYRSNK LIDLRALAVT AVKICGDNKY KLDAMIVVNH
SEKITIPSGA PQPSTSAGPL DIECSWDSEL KQAIGVQSPV EWMDAEDPSF ILYTSGSTGA
PKGIVHTTAG YMTYAYYTCK IVFDSQDDDM YWCTADCGWI TGHSYVVYGP LMNGMSSVIF
EGVPTYPDAG RMWNIVEKYK VTKFYTAPTA VRCLMGFGNE MVSKYDRSSL KIIGSVGEPI
NPAAWEWLYY VVGEEKAAVV DTYWQTETGG HVIVPIPGAI PTKPGSATLP FFGVVPCILD
NDGALMEGPG EGNLCFSRPW PGISRSCWAD HERWEKTYFS SFNGYYFTGD GSKRDDDGYY
WITGRVDDLM NVSGHLLSTA EIESALVAHP DVSEAAVVAA PHDIKGSFPY AFVTMKEGSK
LTPEVVTQLK LTVRRKIGAI AVPDIVQEAP GLPKTRSGKI TRRILRKIAE GDVNADFGDT
TTLVDESVIT KLLSNRPESR TG
//