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Database: UniProt
Entry: A0A1B7TID6_9ASCO
LinkDB: A0A1B7TID6_9ASCO
Original site: A0A1B7TID6_9ASCO 
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}.
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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
//
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