ID A0A1B7MUU9_9AGAM Unreviewed; 661 AA.
AC A0A1B7MUU9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN ORFNames=K503DRAFT_826045 {ECO:0000313|EMBL:OAX36327.1};
OS Rhizopogon vinicolor AM-OR11-026.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX36327.1, ECO:0000313|Proteomes:UP000092154};
RN [1] {ECO:0000313|EMBL:OAX36327.1, ECO:0000313|Proteomes:UP000092154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX36327.1,
RC ECO:0000313|Proteomes:UP000092154};
RG DOE Joint Genome Institute;
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (JUN-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|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; KV448425; OAX36327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7MUU9; -.
DR STRING; 1314800.A0A1B7MUU9; -.
DR InParanoid; A0A1B7MUU9; -.
DR OrthoDB; 144557at2759; -.
DR Proteomes; UP000092154; 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:UP000092154}.
FT DOMAIN 33..89
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 91..478
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 539..621
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 661 AA; 72853 MW; BCE651C20D602B86 CRC64;
MSEPEVVPIH PVAPRLKAGS KVPHIGPDIA AYKAAHAETL GHESDKWWAK MAHEMLHWDR
PFQTVRAGGF ETGDITWFPE GGLNASYNCV DRWAFKHPDK TAIIYEADEP DEGRLITYAE
LLREVSSIAN VLKNMGVKKG DTVSVYLPMT WQAVAAFLAC ARIGAVHSVV FAGFSSESLR
DRVIDCKSRV LLTSDEGRRG GKSVATKLIV DAALKECPLV EHVLVLKRTG NQVPWTEGRD
KWWHEETAKV PNYCPPEIMS SEDPLFILYT SGSTGKPKGV VHTTGGYLLC AALTVKYVFD
VHPDDKFACM ADIGWITGHT YIVYGPLANG VSTTVFESTP VYPTPSRYWQ TVEKHQLTQF
YSAPTAIRLL RRLGAQHVED HDLSSLRVLG SVGEPINPEA WNWYNEHVGK KQCAIVDTFW
QTETGSIVVT PFPGAIETKP GSATVPFFGI EPAILDPVSG KELEGNNVEG VLVLKQPWPS
IARSVYNDHN RYLETYMKPY PGVFYTGDGA ARDEHGYIWI KGRIDDVINV SGHRLSTAEI
ESALIMHKGV AETAVIGTAD ELTGQAVFAF VTLKPEFTYD TNDEASLAKE LVLQVRKVIG
PFAAPKKIFI VSDLPKTRSG KIMRRIMRKI VAGEGDQLGD LSTVAEPGVV DVIKKKVAES
T
//
