ID   ACS2_CANAL              Reviewed;         671 AA.
AC   Q8NJN3; Q59VM9;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Acetyl-coenzyme A synthetase 2;
DE            EC=6.2.1.1;
DE   AltName: Full=Acetate--CoA ligase 2;
DE   AltName: Full=Acyl-activating enzyme 2;
GN   Name=ACS2; ORFNames=CaO19.1064, CaO19.8666;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales;
OC   Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-581.
RA   Jones P.M., Clarkson J.M., Wheals A.E.;
RT   "Acetyl-CoA synthetase 2 of Candida albicans.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
CC       acetyl-CoA.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AACQ01000121; EAK94564.1; -; Genomic_DNA.
DR   EMBL; AACQ01000120; EAK94610.1; -; Genomic_DNA.
DR   EMBL; AF535132; AAN01233.1; -; Genomic_DNA.
DR   RefSeq; XP_713668.1; -.
DR   RefSeq; XP_713713.1; -.
DR   GeneID; 3644652; -.
DR   GeneID; 3644710; -.
DR   CGD; CAL0001207; ACS2.
DR   OMA; Q8NJN3; KEFFERQ.
DR   BRENDA; 6.2.1.1; 1124.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:EC.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   InterPro; IPR011904; Ac_CoA_lig_AcsA.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 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    671       Acetyl-coenzyme A synthetase 2.
FT                                /FTId=PRO_0000208406.
FT   CONFLICT    388    388       A -> V (in Ref. 2; AAN01233).
FT   CONFLICT    576    581       VIAYVA -> ALLTLP (in Ref. 2; AAN01233).
SQ   SEQUENCE   671 AA;  73862 MW;  16FCB5DCC5922275 CRC64;
     MPTEQTHNVV HEANGVKLRE TPKEFFERQP NKGHIHDVNQ YKQMYEQSIK DPQGFFGPLA
     KELLSWDHDF HTVKSGTLKN GDAAWFLGGE LNASYNCVDR HAFANPDKPA LICEADDEKD
     SHILTYGDLL REVSKVAGVL QSWGIKKGDT VAVYLPMNAQ AIIAMLAIAR LGAAHSVIFA
     GFSAGSIKDR VNDASCKALI TCDEGKRGGR TTNIKKLCDE ALVDCPTVEK VLVYKRTNNP
     EIHLTEGRDY YWDVETAKFP GYLPPVSVNS EDPLFLLYTS GSTGTPKGVV HSTAGYLLGA
     ALSTKYIFDI HPEDILFTAG DVGWITGHTY ALYGPLLLGV PTIIFEGTPA YPDYGRFWQI
     VEKHKATHFY VAPTALRLLR KAGEQEIAKY DLSSLRTLGS VGEPISPDIW EWYNEFVGKN
     QCHISDTYWQ TESGSHLIAP LAGVVPNKPG SASYPFFGID AALIDPVTGV EIEGNDAEGV
     LAIKDHWPSM ARTVYKNHTK YMDTYMNPYP GYYFTGDGAA RDHDGYYWIR GRVDDVVNVS
     GHRLSTAEIE AALIEDKKVS EAAVVGIHDD ITGQAVIAYV ALKEGNSDED SEGLRKELVL
     QVRKTIGPFA APKSVIIVQD LPKTRSGKIM RRILRKVSSN EADQLGDIST LSNPQSVEGI
     ISAFGAQFGK K
//