ACS1_CANAX
ID ACS1_CANAX Reviewed; 675 AA.
AC O94049;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Acetyl-coenzyme A synthetase 1;
DE EC=6.2.1.1;
DE AltName: Full=Acetate--CoA ligase 1;
DE AltName: Full=Acyl-activating enzyme 1;
GN Name=ACS1; ORFNames=Ca38F10.03;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1161;
RA Oliver K., Harris D., Barrell B.G., Rajandream M.A.;
RT "Candida albicans strain 1161 genome pilot sequencing project.";
RL Submitted (NOV-1998) 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 -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL033502; CAA22000.1; -; Genomic_DNA.
DR AlphaFoldDB; O94049; -.
DR SMR; O94049; -.
DR CGD; CAL0000184618; ACS1.
DR VEuPathDB; FungiDB:C2_10350C_A; -.
DR VEuPathDB; FungiDB:CAWG_06106; -.
DR GO; GO:0005829; C:cytosol; ISA:CGD.
DR GO; GO:0003987; F:acetate-CoA ligase activity; ISA:CGD.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; ISA:CGD.
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.
FT CHAIN 1..675
FT /note="Acetyl-coenzyme A synthetase 1"
FT /id="PRO_0000208405"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212..215
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 407..409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 431..436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 545
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 609
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT VARIANT 504
FT /note="N -> K"
FT VARIANT 543
FT /note="N -> D"
SQ SEQUENCE 675 AA; 75100 MW; 32CD1F462F789B90 CRC64;
MPESTQQSHL SLDHEKMQQP PKGFTERSKT KPNLADFETY QKLYKQSIEN PNEFFTQQAK
ENLDWFKPFD LARFPVDPKD DYKNGDLPAW FINGQLNACY NAVDRWAIKN PDKPAIIYEG
DEPDQGRIIT YGELLKQVSK LAQALTKLGV KKGDSVAVYL PMIPEAIVTL LAIVRIGAMH
SVVFAGFSSA SLRDRILDAD SRIVITADES KRGGKTIETK KIVDDALKEC PKVRNVIVFK
RTGNSHVPFS PGRDLWWHDE MAKYGPYFPP VPVNSEDPLF LLYTSGSTGK PKGVQHNTAG
YLLGAVLTTK YTFDVHEDDI LFTAGDIGWI TGHTYCVYGP LLAGATSVVF EGTPAYPNYS
RYWEIVDKYK VNQFYVAPTA LRLLKRAGTK YVEKYDLSSL RVLGSVGEPI AAEVWHWYND
NIGRGQAHIV DTYWQTESGS HLLTPLAGIT PTKPGSASLP FFGVDPKILD PTTGEELPDN
DVEGVLAIKS AWPSITRGIY NDYNRFIDTY LAPYANYYFS GDGAARDRDG FYWILGRVDD
VVNVSGHRLS TAEIEAALIE HPIVGESAVV GYADELTGQA VAAYVSLKKD KAVGEDVENI
KKEMILTVRK EIGPFAAPKM ILLVDDLPKT RSGKIMRRIL RKVLAGEEDQ LGDISTLSNP
GVVQQIIDVV HHAKK