ID A0A1B7TID6_9ASCO Unreviewed; 675 AA.
AC A0A1B7TID6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN ORFNames=HANVADRAFT_51403 {ECO:0000313|EMBL:OBA28499.1};
OS Hanseniaspora valbyensis NRRL Y-1626.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=766949 {ECO:0000313|EMBL:OBA28499.1, ECO:0000313|Proteomes:UP000092321};
RN [1] {ECO:0000313|Proteomes:UP000092321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-1626 {ECO:0000313|Proteomes:UP000092321};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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|ARBA:ARBA00000131,
CC ECO:0000256|RuleBase:RU361147};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|RuleBase:RU361147}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBA28499.1}.
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; LXPE01000003; OBA28499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7TID6; -.
DR OrthoDB; 144557at2759; -.
DR Proteomes; UP000092321; 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:SF245; ACETYL-COENZYME A SYNTHETASE 2; 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:UP000092321}.
FT DOMAIN 39..95
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 97..484
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 546..630
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 675 AA; 74361 MW; 5919F1F0B33ABD50 CRC64;
MSNNHVEVHE ANGAAFRYAP DHFFKSQPSA SYIANEEQYR QMYDQSINDP ETFYGNLAKE
YLHWDKPFAK VKSGSLEKGD IAWFLQGELN ACYNCVDRHA FANPNKVALI SEPDEESEAY
SITFQELLEK VCKVAGVLQS WGVKKGDTVA VYLPMTPEAV IAMLAIARIG AVHSVVFAGF
SAGSLKDRVV DAGCKVVITC DEAKRGGKTI NTKKIVDEGL NGVQSVSHIL VFKRTGNPAV
NMTPGRDFYW DEACAHQRSY IPCVSTNAED PLFLLYTSGS TGQPKGVVHT VGGYLLNSAL
STRFVFDLHP EDVFFTAGDV GWITGHTYAL YGPLSLGTAT IIFESTPAYP DYGRYWRIVS
KWKATHFYVA PTAMRLIKKV GEQEIDKYDI SSLRVLGSVG EPIQPDLWEW YNEKIGHNNC
CIVDTYWQTE SGAHLITPLA GVFPTKAGAA SLPFFGIAPA IIDPNTGKEL EGNDVSGVLA
VKSTWPSMAR SVFNDHQRYI DTYLKPFAGY YFTGDNAARD NDGYYWIRGR ADDVVNVSGH
RLSTNEIETV LDEHDGVSEC ACIGVNDDLT GQAVIAFLSL KEGACDISDE HVFMGFKKSL
VMEVRGSIGP FASPKAIIVV DDLPKTRSGK IMRRVLRKIA SNEAEQIGDL STMANAECIP
RILSAVDNQF LSKKK
//