ACS2_CANGA
ID ACS2_CANGA Reviewed; 683 AA.
AC Q6FXI2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=CAGL0B02717g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR380948; CAG57989.1; -; Genomic_DNA.
DR RefSeq; XP_445089.1; XM_445089.1.
DR AlphaFoldDB; Q6FXI2; -.
DR SMR; Q6FXI2; -.
DR STRING; 5478.XP_445089.1; -.
DR PRIDE; Q6FXI2; -.
DR EnsemblFungi; CAG57989; CAG57989; CAGL0B02717g.
DR GeneID; 2886546; -.
DR KEGG; cgr:CAGL0B02717g; -.
DR CGD; CAL0127800; CAGL0B02717g.
DR VEuPathDB; FungiDB:CAGL0B02717g; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; Q6FXI2; -.
DR OMA; SPDIWEW; -.
DR Proteomes; UP000002428; Chromosome B.
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..683
FT /note="Acetyl-coenzyme A synthetase 2"
FT /id="PRO_0000208408"
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"
SQ SEQUENCE 683 AA; 75551 MW; 89C07BF8ECD26766 CRC64;
MTLKEHKTVH EAQNAVARQA PEHFYKSQPS RGGFIKDISE YERLYKQSIE DPETFFSEKA
RELLHWDAPF SKVSYGSLEQ GDVAWFLNGK LNASYNCVDR HAFANPDKPA IIYEADDEKD
NYTITFGELL RRVSKVAGIL KSWGVKKGDT VAIYLPMIPE AIIAMLAVVR LGAIHSVVFA
GFSAGSLKDR VVDAGSKVVI TCDEGRRGGK TVHLKKIVDE GLNGVDQVSR ILVFKRTGTE
GIPMKAGRDF WLHEEADKRR SYLPPVPCDA EDPLFLLYTS GSTGSPKGIV HTTGGYLLGA
AMTTKYVFDV HPEDVFFTAG DVGWITGHTY ALYGPLLLGV PTICFESTPA YPDYGRYWRI
VERHKATHFY VAPTAMRLIK RVGEAEISKY DLSSLRVLGS VGEPISPELW EWYNEKIGNN
NCVVCDTFWQ TESGSHLIAP MAGAIPTKPG STTLPFFGID ACIIDPVSGV EIEGNDVEGV
LAVKSPWPSM ARSVWNDHVR YVDTYMKPYP GYYFTGDGAG RDHDGYYWIR GRVDDVVNVS
GHRLSTAEIE ACLVNHENIS ETAVVGINDE LTGQAVIAFV SLKEGYLQND APEGDAEHIT
PSNLRRELIL QVRGEIGPFA SPKCIILVRD LPKTRSGKIM RRVLRKIASN EADQLGDLST
LANADVVPAI ISACENQFFA EKK
