ID   A0A165A4R4_XYLHT        Unreviewed;       667 AA.
AC   A0A165A4R4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE            EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN   ORFNames=L228DRAFT_214050 {ECO:0000313|EMBL:KZF19947.1};
OS   Xylona heveae (strain CBS 132557 / TC161).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC   Xylonales; Xylonaceae; Xylona.
OX   NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF19947.1, ECO:0000313|Proteomes:UP000076632};
RN   [1] {ECO:0000313|EMBL:KZF19947.1, ECO:0000313|Proteomes:UP000076632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC161 {ECO:0000313|EMBL:KZF19947.1,
RC   ECO:0000313|Proteomes:UP000076632};
RX   PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA   Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA   Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The genome of Xylona heveae provides a window into fungal endophytism.";
RL   Fungal Biol. 120:26-42(2016).
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}.
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DR   EMBL; KV407464; KZF19947.1; -; Genomic_DNA.
DR   RefSeq; XP_018185502.1; XM_018330020.1.
DR   AlphaFoldDB; A0A165A4R4; -.
DR   STRING; 1328760.A0A165A4R4; -.
DR   GeneID; 28895157; -.
DR   InParanoid; A0A165A4R4; -.
DR   OMA; INVSYNC; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000076632; 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: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:SF14; ACETYL-COENZYME A SYNTHETASE 1; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076632}.
FT   DOMAIN          42..98
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          100..485
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          547..625
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   667 AA;  74250 MW;  700CE9D9A282AE65 CRC64;
     MPEGEAKAPA AHEYNPHEVY PVPQGLFKKH STRPHLINLE EYRKLHKESI ENPDKFWAKQ
     ARELLTWERD FQTVRSGSLT NGDIAWFLEG RLNASYNCVD RHAFKDPEKP AILYEADEPG
     DGRIITYGEL LRQVSKLAYV LKQMGVKKGD TVAIYLPMIP EALIAFLACS RIGAVHSVIF
     AGFSSDSLRD RVLDAQSKVV ITTDEGRRGG KVIGTKKIVD DALKQCPDVS HVLVYRRTGA
     EIPWTKGRDF WWHEEVEKYP SYIAPEPVNS EDPLFLLYTS GSTGKPKGVM HTTAGYLLGA
     ASTGKYVFDI HDTDRFFCGG DVGWITGHTY VVYAPLLLGV ATVVFEGTPA YPDFSRYWEV
     IEKYSVTQFY VAPTALRLLK RAGDHHVKHK MKGLRVLGSV GEPIAAEVWK WYYEVVGKEE
     AHVVDTYWQT ETGCHAITPL AGITPSKPGS ATLPFFGFDP VIIDPVSGEE IQGNDVEGVL
     AFKQAWPSIA RTVWGAHKRY MDTYLNVYKG YYFTGDGAGR DHDGYYWIRG RVDDVVNVSG
     HRLSTAEIEA ALIEHHAVGE AAVVGIHDEL TGQAVNAFVS LKDEQSSLDQ VKKELVLQVR
     KSIGPFAAPK AVYIVGDLPK TRSGKIMRRI LRKILAGEED SLGDTSTLSD PSVVDKILDL
     VHSSRKN
//