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Database: UniProt
Entry: B8EPJ0
LinkDB: B8EPJ0
Original site: B8EPJ0 
ID   ACSA_METSB              Reviewed;         645 AA.
AC   B8EPJ0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   26-NOV-2014, entry version 38.
DE   RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE            Short=AcCoA synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE            Short=Acs {ECO:0000255|HAMAP-Rule:MF_01123};
DE            EC=6.2.1.1 {ECO:0000255|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acetate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_01123};
DE   AltName: Full=Acyl-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01123};
GN   Name=acsA {ECO:0000255|HAMAP-Rule:MF_01123};
GN   OrderedLocusNames=Msil_1226;
OS   Methylocella silvestris (strain BL2 / DSM 15510 / NCIMB 13906).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Beijerinckiaceae; Methylocella.
OX   NCBI_TaxID=395965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL2 / DSM 15510 / NCIMB 13906;
RX   PubMed=20472789; DOI=10.1128/JB.00506-10;
RA   Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA   Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT   "Complete genome sequence of the aerobic facultative methanotroph
RT   Methylocella silvestris BL2.";
RL   J. Bacteriol. 192:3840-3841(2010).
CC   -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA
CC       (AcCoA), an essential intermediate at the junction of anabolic and
CC       catabolic pathways. AcsA undergoes a two-step reaction. In the
CC       first half reaction, AcsA combines acetate with ATP to form
CC       acetyl-adenylate (AcAMP) intermediate. In the second half
CC       reaction, it can then transfer the acetyl group from AcAMP to the
CC       sulfhydryl group of CoA, forming the product AcCoA.
CC       {ECO:0000255|HAMAP-Rule:MF_01123}.
CC   -!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
CC       acetyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01123}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01123};
CC   -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC       activates the enzyme. {ECO:0000255|HAMAP-Rule:MF_01123}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000255|HAMAP-Rule:MF_01123}.
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DR   EMBL; CP001280; ACK50195.1; -; Genomic_DNA.
DR   RefSeq; YP_002361557.1; NC_011666.1.
DR   ProteinModelPortal; B8EPJ0; -.
DR   STRING; 395965.Msil_1226; -.
DR   EnsemblBacteria; ACK50195; ACK50195; Msil_1226.
DR   GeneID; 7092299; -.
DR   KEGG; msl:Msil_1226; -.
DR   PATRIC; 22597937; VBIMetSil55537_1347.
DR   eggNOG; COG0365; -.
DR   HOGENOM; HOG000229981; -.
DR   KO; K01895; -.
DR   OMA; AWIWYRD; -.
DR   OrthoDB; EOG68WR2H; -.
DR   BioCyc; MSIL395965:GCND-1250-MONOMER; -.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR   HAMAP; MF_01123; Ac_CoA_synth; 1.
DR   InterPro; IPR011904; Ac_CoA_lig.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
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   Acetylation; ATP-binding; Complete proteome; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    645       Acetyl-coenzyme A synthetase.
FT                                /FTId=PRO_1000164051.
FT   NP_BIND     385    387       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   NP_BIND     409    414       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   REGION      190    193       Coenzyme A binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01123}.
FT   METAL       535    535       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   METAL       537    537       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   METAL       540    540       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   BINDING     309    309       Coenzyme A. {ECO:0000255|HAMAP-
FT                                Rule:MF_01123}.
FT   BINDING     498    498       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   BINDING     513    513       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   BINDING     521    521       Coenzyme A; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   BINDING     524    524       ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
FT   BINDING     582    582       Coenzyme A. {ECO:0000255|HAMAP-
FT                                Rule:MF_01123}.
FT   MOD_RES     607    607       N6-acetyllysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01123}.
SQ   SEQUENCE   645 AA;  70912 MW;  79DAA68C78D3C927 CRC64;
     MSDKVYPVTA EWSKSAYVDA AKYKSMYESS VSEPDKFWGE HGKRIDWVKP YTKVKNTSFD
     PHNVSIKWFE DGVTNVSTNC IDRHLATLGD QTAIIWEGDD PNESKHITYK QLHEEVCRLA
     NVLKSYGISK GDTVTIYLPM IPEAAYAMLA CARIGAIHSI VFGGFSADSL GGRIEGCKSK
     LIITADEGYR GGRKVPLKVN ADAAIKKVDG IVETMIVVRR TGGKVAWTEG RDVWYDEALA
     KASPDCPAAE MNAEDPLFIL FTSGSTGAPK GVVHSTGGYL VWASMTHQYV FDYRPGEVYW
     CTADVGWVTG HSYIVYGPLA NGATTLMFEG VPSYPTISRF WDVVDKHQVN IFYTAPTAIR
     SLMGAGDGPV KATSRKTLRV LGSVGEPINP EAWEWYYRVV GEERCPIVDT WWQTETGGIL
     ISPLPGATAL KPGSATQPFF GVQPQVVDAA GEVLEGPCSG NLVIADSWPA QMRTLFNDHE
     RFVQAYFSAY PGKYFTGDGC RRDEDGYYWI TGRVDDVINV SGHRLGTAEV ESSLVAHIKV
     AEAAVVGYPH DLKGQGIYAY VTLMTGIEPS EELRKELVSW VRKDIGPIAS PDIVHFAPGL
     PKTRSGKIMR RILRKIAEKE FSALGDTSTL ADPSVVDDLI RERAN
//
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