ID C5MF86_CANTT Unreviewed; 671 AA.
AC C5MF86;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|RuleBase:RU361147};
DE EC=6.2.1.1 {ECO:0000256|RuleBase:RU361147};
GN ORFNames=CTRG_04729 {ECO:0000313|EMBL:EER31946.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER31946.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER31946.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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}.
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DR EMBL; GG692400; EER31946.1; -; Genomic_DNA.
DR RefSeq; XP_002550431.1; XM_002550385.1.
DR AlphaFoldDB; C5MF86; -.
DR STRING; 294747.C5MF86; -.
DR EnsemblFungi; CTRG_04729-t43_1; CTRG_04729-t43_1-p1; CTRG_04729.
DR GeneID; 8298082; -.
DR KEGG; ctp:CTRG_04729; -.
DR VEuPathDB; FungiDB:CTRG_04729; -.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_6_1; -.
DR OrthoDB; 144557at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016880; F:acid-ammonia (or amide) ligase activity; IEA:EnsemblFungi.
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:UP000002037}.
FT DOMAIN 42..98
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 100..487
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 549..628
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 671 AA; 73892 MW; 98CE6E4458B8C1DF CRC64;
MTTESNNHKV VHEANGVQLR ETPKEFFQRQ PNKGHIQDTE EYKKMYEQSI KDPQGFFGPL
AKELLSWDSD FHTVKSGTLK NGDAAWFLGG KLNASYNCVD RHALANPNKP AIIYEADEEK
DSYILTYGDL LREVSKVAGV LHSWGVRKGD TVAVYLPMNA QALIAMLAIA RLGAAHSVIF
AGFSSGSIKD RVNDASCKAL ITCDEGRRGG RTTNIKKLCD EALKQCPTVQ KVLVHRRTGN
PDIKLVEGRD YYWDEETAKF SGYFPPVAVD SEDPLFLLYT SGSTGTPKGV VHSTAGYLLG
AALTTKYIFD VHPEDIFFTA GDVGWITGHT YALYGPLLLG VPSVVFEGTP AYPDYGRFWQ
IVEKHKATHF YVAPTALRLL RKAGEQEIAK YDLSSLRTLG SVGEPISPDI WEWYNEFVGK
DQCHISDTYW QTESGSHLIA PLAGVIANKP GSASYPFFGI DAALIDPVSG VEITGNDVEG
VLVVKDHWPS MARTVFNNHV KYMDTYMNPY PGYYFTGDGA ARDNDGYYWI RGRVDDVVNV
SGHRLSTAEI ESALIEDPRV GESAVVGIND DLTGQAVVAY VALKTGDVPD EDALRKELIL
LVRKEIGPFA APKSVILVQD LPKTRSGKIM RRILRKVSSN EADQLGDITT LQNPGSVEGI
ISAFSAQFGR K
//