ACS2_KLULA
ID ACS2_KLULA Reviewed; 684 AA.
AC Q9Y7B5; Q6CQG2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=KLLA0D17336g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC MYA-539 / JBD100;
RX PubMed=12489122; DOI=10.1002/yea.936;
RA Zeeman A.-M., Steensma H.Y.;
RT "The acetyl co-enzyme A synthetase genes of Kluyveromyces lactis.";
RL Yeast 20:13-23(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; AF134491; AAD30108.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH00923.1; -; Genomic_DNA.
DR RefSeq; XP_453827.1; XM_453827.1.
DR AlphaFoldDB; Q9Y7B5; -.
DR SMR; Q9Y7B5; -.
DR STRING; 28985.XP_453827.1; -.
DR EnsemblFungi; CAH00923; CAH00923; KLLA0_D17336g.
DR GeneID; 2893299; -.
DR KEGG; kla:KLLA0_D17336g; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; Q9Y7B5; -.
DR OMA; SPDIWEW; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
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: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..684
FT /note="Acetyl-coenzyme A synthetase 2"
FT /id="PRO_0000208415"
FT BINDING 207..210
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 402..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 426..431
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 613
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT CONFLICT 491
FT /note="A -> D (in Ref. 1; AAD30108)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 684 AA; 75105 MW; 9B62655F72CFAA8E CRC64;
MSSDKLHKVV HEAHDVEARH APEHFYNSQP GKSYCTDEEH YREMYTQSIE DPAGFFGPLA
KEYLDWDRPF TQVQSGSLEH GDIAWFLNGE LNASYNCVDR HAFANPDKPA LIYEADDESE
NKVITFGELL RQVSEVAGVL QSWGVKKGDT VAVYLPMIPA AVVAMLAVAR LGAIHSVIFA
GFSAGSLKER VVDAGCKVVI TCDEGKRGGK TVHTKKIVDE GLAGVDSVSK ILVFQRTGTQ
GIPMKPARDF WWHEECVKQR GYLPPVPVNS EDPLFLLYTS GSTGSPKGVV HSTAGYLLGS
ALTTRFVFDI HPEDVLFTAG DVGWITGHTY ALYGPLTLGT ATIIFESTPA YPDYGRYWRI
IERHRATHFY VAPTALRLIK RVGEEEIAKY DTSSLRVLGS VGEPISPDLW EWYHEKVGKN
NCVICDTMWQ TESGSHLIAP LAGAVPTKPG SATVPFFGIN ACIIDPVSGE ELKGNDVEGV
LAVKSPWPSM ARSVWNNHAR YFETYLKPYP GYYFTGDGAG RDHDGYYWIR GRVDDVVNVS
GHRLSTAEIE AALAEHEGVS EAAVVGITDE LTGQAVIAFV SLKDGYLSEN AVEGDSTHIS
PDNLRRELIL QVRGEIGPFA APKTVVVVND LPKTRSGKIM RRVLRKVASK EADQLGDLST
LANADVVPSI ISAVENQFFS QQKK
