ACS2_ASHGO
ID ACS2_ASHGO Reviewed; 687 AA.
AC Q750T7;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Acetyl-coenzyme A synthetase 2;
DE EC=6.2.1.1;
DE AltName: Full=Acetate--CoA ligase 2;
DE AltName: Full=Acyl-activating enzyme 2;
GN Name=ACS2; OrderedLocusNames=AGL148C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AE016820; AAS54343.1; -; Genomic_DNA.
DR RefSeq; NP_986519.1; NM_211581.1.
DR AlphaFoldDB; Q750T7; -.
DR SMR; Q750T7; -.
DR STRING; 33169.AAS54343; -.
DR EnsemblFungi; AAS54343; AAS54343; AGOS_AGL148C.
DR GeneID; 4622812; -.
DR KEGG; ago:AGOS_AGL148C; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; Q750T7; -.
DR OMA; SPDIWEW; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0016880; F:acid-ammonia (or amide) ligase activity; IEA:EnsemblFungi.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR GO; GO:0016573; P:histone acetylation; IEA:EnsemblFungi.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 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.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..687
FT /note="Acetyl-coenzyme A synthetase 2"
FT /id="PRO_0000208404"
FT BINDING 206..209
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 401..403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 425..430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 617
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
SQ SEQUENCE 687 AA; 75369 MW; E7099F544E8F77C7 CRC64;
MSCKEHKVVH EAHNVEARKT PDHFYRSQPG PSYVQDIEQY RTMYQQSIED PDAFFGEKAR
EFLHWEKDFT HVRAGSLRTG DTAWFLNGEL NAAYNCVDRH ALENPDKVAI IYEADDEADN
RVVTFGELLR QVSQVAGVLQ SWGVKKGDTV AVYMPMIPEA VVAMLAVARL GAVHSVIFAG
FSSGSLRDRI VDAESKVVIT CDEGRRGGKT VHTKKIVDEG LAGVGVVSHI LVFQRTGSEG
IPMKAGRDFW WHEEVRKQRG YLPPVSVNAE DPIFLLYTSG STGSPKGVVH TTGGYLLGAA
LTTRYVFDIH PEDVLFTAGD VGWITGHTYA LYGPLCLGTA TIIFESTPAY PDYGRYWRII
QRHKATHFYV APTAMRLIKT VGEQEISKYD LSSLRVLGSV GEPIAPDLWE WYNEKVGNNN
CVVCDTMWQT ESGSHLIAPL AGAIPTKPGS ATVPFFGINA CIIDPVTGDE LEGNDVEGVL
AIKSPWPSMA RSVWNNHDRY IETYLKPYPG YYFTGDGAGR DHDGYYWIRG RVDDVVNVSG
HRLSTAEIEA ALSEHEGVSQ AAVVGIADEL TGQAVVAFVS LKEGYGRGSS TDTDPESIAP
DVVPLDTLRR ELVLQVRAEI GPFAAPKSVI VVDDLPKTRS GKIMRRTLRK ISANEADQLG
DLSTLANPET VPAIIAAVGA QFLKGKK
