ACS2_DEBHA
ID ACS2_DEBHA Reviewed; 679 AA.
AC Q6BS00;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=DEHA2D12606g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382136; CAG87188.1; -; Genomic_DNA.
DR RefSeq; XP_459020.1; XM_459020.1.
DR AlphaFoldDB; Q6BS00; -.
DR SMR; Q6BS00; -.
DR STRING; 4959.XP_459020.1; -.
DR PRIDE; Q6BS00; -.
DR EnsemblFungi; CAG87188; CAG87188; DEHA2D12606g.
DR GeneID; 2901554; -.
DR KEGG; dha:DEHA2D12606g; -.
DR VEuPathDB; FungiDB:DEHA2D12606g; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR InParanoid; Q6BS00; -.
DR OMA; SPDIWEW; -.
DR OrthoDB; 288915at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
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 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..679
FT /note="Acetyl-coenzyme A synthetase 2"
FT /id="PRO_0000208412"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 611
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
SQ SEQUENCE 679 AA; 74992 MW; AD17F7989E476776 CRC64;
MTSSPTHQVV HEANNIKKQE TPKEFFERQP RQGHITSLEQ YQELYEKSIN DPETFFGEFG
KELLHWDRDF ERVKSGSLLH GDAAWFIGGQ LNACYNCVDR HAFATPNKPA IIYEADEEKD
SKILTFAELL REVCQVAGVL QSWGIKKGDT VAIYMPMNSQ AIIAMLAVAR LGAIHSVIFA
GFSSGSIKDR VNDASCKALI TCDEGRRGGK TINIKKLCDE ALLNCPSIEK VLVYERTGNK
EVTLKEGRDY WWSEETQKFA GYLPPVPVNS EDPLFLLYTS GSTGTPKGVV HSTAGYLLGA
ALTTKYVFDI HPEDVLFTAG DVGWITGHTY ALYGPLSLGV PTVVFEGTPA FPDYGRLWQI
VEKHKATHFY VAPTALRLLR KSGEQEIEKY DLSSLRTLGS VGEPISPDIW EWYNEKVGKG
QCHVTDTYWQ TESGSHFIAP IAGVVPNKPG SAAVPFFGIQ TCLIDPVSGI EIQGNDVEGV
LAVKDTWPSM ARSVYKNHTK YMDTYLNPYP GYYFTGDGAA RDHDGYYWIR GRVDDVVNVS
GHRLSTAEIE AALIEHNAIS EAAVVGMNDD LTGQTVVAFV ALKEHLIANL KADESPEEAL
KLKKEMILQV RTQIGPFAAP KSVIIVEDLP KTRSGKIMRR ILRKIAAGEA DQLGDITTLS
NPQSVAGIIG SFDSQFGKK
