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
//