ID A0A1L0DRI2_9ASCO Unreviewed; 672 AA.
AC A0A1L0DRI2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN ORFNames=SAMEA4029009_CIC11G00000004512 {ECO:0000313|EMBL:SGZ58360.1},
GN SAMEA4029010_CIC11G00000000954 {ECO:0000313|EMBL:SGZ53516.1};
OS [Candida] intermedia.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ58360.1, ECO:0000313|Proteomes:UP000182259};
RN [1] {ECO:0000313|Proteomes:UP000182259, ECO:0000313|Proteomes:UP000182334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ53516.1,
RC ECO:0000313|Proteomes:UP000182334}, and PYCC 4715
RC {ECO:0000313|EMBL:SGZ58360.1, ECO:0000313|Proteomes:UP000182259};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|RuleBase:RU361147};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU361147}.
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DR EMBL; LT635759; SGZ53516.1; -; Genomic_DNA.
DR EMBL; LT635769; SGZ58360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L0DRI2; -.
DR STRING; 45354.A0A1L0DRI2; -.
DR OrthoDB; 144557at2759; -.
DR Proteomes; UP000182259; Chromosome vi.
DR Proteomes; UP000182334; Chromosome iv.
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:SF14; ACETYL-COENZYME A SYNTHETASE 1; 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:UP000182334}.
FT DOMAIN 35..97
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 99..493
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 548..631
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 672 AA; 74231 MW; 172F22470EA9C22E CRC64;
MPEQLVMDHE KAQDPPKGFF ERSSSKPNLG SLDEYKEMYK QSIEDPATFF GEQAKKLLAW
DRPFDIARHP ESIKDDFKDG DLPAWFLGGQ LNACYNAVDR WAIETPDKAA IIYEGDEPDT
GAIITYAELL KQVCKLAAAL VKLGVKKGDT VAVYLPMIPE AIVTLLAITR IGAVHSVVFA
GFSSTSLKDR IVDADSRLVI TADESKRGGK TIETKKIVDE ALKELPQVRN VLVFKRTGSS
HVPFNAGRDL WWHEELAKYG NYFPPTPVNS EDPLFLLYTS GSTGKPKGIQ HNTAGYLLGA
LLTTKYTFDV HQDDILFTAG DVGWITGHTY VVYGPLLNGA TTVVFEGTPA YPDFSRYWQI
VDKYKVNQFY VAPTALRLLK RAGTSFIEKY KLDSIRVLGS VGEPIAAEVW HWYNDNIGRG
KAHIVDTYWQ TESGSHLLTP LSGITPTKPG SASLPFFGID AHILDPVTGE ELLEDGVEGV
LAIKNAWPSI ARGIFNDYNR FIDTYLGAYP GYYFTGDGAA RDKDGFYWIL GRVDDVVNVS
GHRLSTAEIE AALIEHQMVA ESAVVGYADE LTGQAVAAYV SLKSNFKADD KESIDAVKKE
LILTVRKEIG PFAAPKLILL VDDLPKTRSG KIMRRILRKV LAGEEDQLGD ISTLSNPGVV
LQIIDVVKLT RK
//
