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 01-MAY-2013, entry version 30.
DE RecName: Full=Acetyl-coenzyme A synthetase;
DE Short=AcCoA synthetase;
DE Short=Acs;
DE EC=6.2.1.1;
DE AltName: Full=Acetate--CoA ligase;
DE AltName: Full=Acyl-activating enzyme;
GN Name=acsA; 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;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Forester B., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Dunfield P.F.,
RA Dedysh S.N., Liesack W., Stott M.B., Smirnova A.V., Alam M., Chen Y.,
RA Murrell J.C., Richardson P.;
RT "Complete sequence of Methylocella silvestris BL2.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
CC acetyl-CoA.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC activates the enzyme (By similarity).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC family.
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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; PPIKRSC; -.
DR ProtClustDB; PRK00174; -.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA: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; IPR024597; Acyl-CoA_synth_DUF3448.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR025110; DUF4009.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF11930; DUF3448; 1.
DR Pfam; PF13193; DUF4009; 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.
FT CHAIN 1 645 Acetyl-coenzyme A synthetase.
FT /FTId=PRO_1000164051.
FT REGION 409 414 Substrate binding (By similarity).
FT ACT_SITE 515 515 By similarity.
FT METAL 535 535 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 537 537 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 540 540 Magnesium; via carbonyl oxygen (By
FT similarity).
FT BINDING 309 309 Coenzyme A (By similarity).
FT BINDING 385 385 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 498 498 Substrate (By similarity).
FT BINDING 513 513 Substrate (By similarity).
FT BINDING 521 521 Coenzyme A (By similarity).
FT BINDING 524 524 Substrate (By similarity).
FT BINDING 582 582 Coenzyme A.
FT MOD_RES 607 607 N6-acetyllysine (By similarity).
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
//
