ID M3JWY7_CANMX Unreviewed; 670 AA.
AC M3JWY7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
DE Flags: Fragment;
GN ORFNames=G210_2807 {ECO:0000313|EMBL:EMG46924.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG46924.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG46924.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:EMG46924.1}.
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; AOGT01001823; EMG46924.1; -; Genomic_DNA.
DR AlphaFoldDB; M3JWY7; -.
DR STRING; 1245528.M3JWY7; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR OMA; TVHTKKI; -.
DR OrthoDB; 144557at2759; -.
DR Proteomes; UP000011777; 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:UP000011777}.
FT DOMAIN 41..97
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 99..486
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 548..627
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMG46924.1"
SQ SEQUENCE 670 AA; 73879 MW; EE7B0E04E954C99F CRC64;
MTTESTHKVV HEANGVKLRQ TPKEFFERQP NKGFIKDIDH YKELYEKSIK DPEGFFGPLA
KEMLSWDHDF HTVKSGTLKE GNPAWFLGGE LNASFNCVDR HALANPDKPA IIYEADEEKD
SYILTYGQLL QEVSKVAGVL KSWGIKKGDN VAIYLPMNVH AIVAMLAVTR LGAAHSVIFA
GFSSGSIRDR VNDASCKALI TCDEGRRGGR TTNIKKLCDE ALGSCPTVEK VLVHRRTGNP
EIKLTEGRDF YWDVETAKFP GYLPPVPVNS EDPLFLLYTS GSTGTPKGVV HTTAGFLLGA
ALTTKYVFDV HPEDIFFTAG DVGWITGHSY ALYGPLLLGV PTVVFEGTPA YPDFGRFWQI
IEKHKATHFY VAPTALRMLR KSGEKETGKY DLSSLRTLGS VGEPISPDIW EWYNEFIGKD
QCHISDTYWQ TESGSHLIAP LAGVTANKPG SASYPFFGIE AALIDPVSGV EITENDVEGV
LVVKDHWPSM ARTVYNNHTK YMDTYLNPYP GYYFTGDGAA RDNDGYYWIR GRVDDVVNVS
GHRLSTAEIE AALIEDKKVS EAAVVGISDD ITGQAVVAFV ALKEGHVADE DALRKELVLL
VRKEIGPFAA PKSVIIVQDL PKTRSGKIMR RILRKISSNE ADQLGDITTL SNPQSVEGII
ESFAAQFGKK
//
