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Database: UniProt
Entry: A0A074WGA9_9PEZI
LinkDB: A0A074WGA9_9PEZI
Original site: A0A074WGA9_9PEZI 
ID   A0A074WGA9_9PEZI        Unreviewed;       670 AA.
AC   A0A074WGA9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE            EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN   ORFNames=M436DRAFT_84183 {ECO:0000313|EMBL:KEQ70604.1};
OS   Aureobasidium namibiae CBS 147.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ70604.1, ECO:0000313|Proteomes:UP000027730};
RN   [1] {ECO:0000313|EMBL:KEQ70604.1, ECO:0000313|Proteomes:UP000027730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ70604.1,
RC   ECO:0000313|Proteomes:UP000027730};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
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; KL584716; KEQ70604.1; -; Genomic_DNA.
DR   RefSeq; XP_013424947.1; XM_013569493.1.
DR   AlphaFoldDB; A0A074WGA9; -.
DR   STRING; 1043004.A0A074WGA9; -.
DR   GeneID; 25417303; -.
DR   HOGENOM; CLU_000022_3_6_1; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000027730; 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:UP000027730}.
FT   DOMAIN          46..102
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          104..489
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          551..629
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   670 AA;  74375 MW;  43C3699B4795BB81 CRC64;
     MSDGDVKPPT SSVVPEAHEV DTYHVPKAFF DKHPDSKPHL DGLDHYRELW KESIEKPDQF
     WGRMARDLLT WDRDFQTVHS GSLENGDNAW FVEGRLNASY NCVDRHAFKN PDKTAIIYEA
     DEVNEGRKIS YGELLREVCR LAYTLKQMGV KKGDTVALYM PMIPEAVIAF LACSRIGAVH
     SVVFAGFSSD SLKDRIIDAD TKVVITTDEG RRGGKLIGTK KIVDDALSKC PDIKHCLVYK
     RTGADVPMTE GRDLWWHEEV EKYPNYIAPE PMNSEDPLFL LYTSGSTGKP KGVMHTTGGY
     LLGAAATGKY VFDIHDQDIF FCGGDVGWIT GHTYVVYAPL LLGVATVVFE GTPAYPDFSR
     YWDVVAQHKV TQFYVAPTAL RLLKRAGDHF VKHEMEHLRV LGSVGEPIAA EVWKWYFEIV
     GKEEAHIVDT YWQTETGSHV ITPLAGVTPT KPGSASLPFF GIEPAIIDPV SGEELHGNDV
     EGVLAFKQAW PSMARTVWGA HKRYMDTYLN VYKGYYFTGD GAARDHEGYY WIRGRVDDVV
     NVSGHRLSTA EIEAALIEHN AVAEAAVVGV ADELTGQAVA AFVAIKNGNE ANDALRKDLI
     MQVRKSIGPF AAPKAIHVVP DLPKTRSGKI MRRILRKILA GEEDQLGDIT TLSDPSVVEK
     IIEVVHASKK
//
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