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Database: UniProt
Entry: A0A167BYL8_9ASCO
LinkDB: A0A167BYL8_9ASCO
Original site: A0A167BYL8_9ASCO 
ID   A0A167BYL8_9ASCO        Unreviewed;       655 AA.
AC   A0A167BYL8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, 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};
GN   Name=ACS2 {ECO:0000313|EMBL:ANB10986.1};
GN   ORFNames=AWJ20_3780 {ECO:0000313|EMBL:ANB10986.1};
OS   Sugiyamaella lignohabitans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Trichomonascaceae; Sugiyamaella.
OX   NCBI_TaxID=796027 {ECO:0000313|EMBL:ANB10986.1, ECO:0000313|Proteomes:UP000189580};
RN   [1] {ECO:0000313|EMBL:ANB10986.1, ECO:0000313|Proteomes:UP000189580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10342 {ECO:0000313|EMBL:ANB10986.1,
RC   ECO:0000313|Proteomes:UP000189580};
RA   Bellasio M., Peymann A., Valli M., Sipitzky M., Graf A., Sauer M., Marx H.,
RA   Mattanovich D.;
RT   "Complete genome sequence and transcriptome regulation of the pentose
RT   utilising yeast Sugiyamaella lignohabitans.";
RL   Submitted (FEB-2016) 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|ARBA:ARBA00000131,
CC         ECO:0000256|RuleBase:RU361147};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|RuleBase:RU361147}.
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DR   EMBL; CP014500; ANB10986.1; -; Genomic_DNA.
DR   RefSeq; XP_018733463.1; XM_018880810.1.
DR   AlphaFoldDB; A0A167BYL8; -.
DR   GeneID; 30035839; -.
DR   KEGG; slb:AWJ20_3780; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000189580; Chromosome c.
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:SF245; ACETYL-COENZYME A SYNTHETASE 2; 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:UP000189580}.
FT   DOMAIN          29..85
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          87..474
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          535..613
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   655 AA;  72341 MW;  B6EBD89165C15C23 CRC64;
     MTALLRQGCY SKLWRKHPSK THLSSFDHYS QLYKESIENP DKFFGDAARE LLSWDRDFKT
     VSSGGFEHGD VAWFLEGQLN ASYNCVDRHA FANPEKIALI YEADDAKDSR NVTYGELLRQ
     VSKLAAVLTS FGVKKGDTVA IYLPNIPEAI VALLAVTRIG AIHSVIFAGF SSGSLKDRIN
     DAKCKVIITS DEGRRGGKTV YTKKIVDDSL KNAPSIEKVL VFKRTGSEIP WTEGRDFWWH
     EELDKQRAYS PPVAVNSEDP LFLLYTSGST GSPKGVVHST AGYLLGAAIT AKHVFDIQEK
     DILFTAGDVG WITGHTYALY APLLLGATSV IFEGTPAYPN LSRYWQIIEK YKVTQFYVAP
     TALRLLKRGG EEFITGHDLS SLRTLGSVGE PIAGEIWEWY HELIGNSECH IADTYWQTET
     GSHIIAPLAG ITPMKPGSAS FPFFGIDLAI IDPVTGKELV GNDVEGVLAV KKPWPSIARS
     VWGAHQRYLD TYLKPYPGLY FTGDGAARDH EGFYWIRGRV DDVVNVSGHR LSTAEIEASL
     IEHHSVAESA VVGVSDDLTG QAVIAFVSLK DGFDHTQEIK KELIMHVRKE IGPFAAPKTV
     IVIDDLPKTR SGKIMRRILR KIVSNEADSI GDISTLNNPQ SVDQIIAAVD IQLKK
//
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