ID ACSA_STRCO Reviewed; 651 AA.
AC Q9X928;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 01-MAY-2013, entry version 72.
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=SCO3563; ORFNames=SCH5.26;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Streptomycineae; Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces
RT coelicolor A3(2).";
RL Nature 417:141-147(2002).
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; AL939117; CAB38500.1; -; Genomic_DNA.
DR PIR; T36684; T36684.
DR RefSeq; NP_627761.1; NC_003888.3.
DR ProteinModelPortal; Q9X928; -.
DR SMR; Q9X928; 15-643.
DR STRING; 100226.SCO3563; -.
DR EnsemblBacteria; CAB38500; CAB38500; CAB38500.
DR GeneID; 1098999; -.
DR KEGG; sco:SCO3563; -.
DR PATRIC; 23736870; VBIStrCoe124346_3619.
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; Reference proteome.
FT CHAIN 1 651 Acetyl-coenzyme A synthetase.
FT /FTId=PRO_0000208389.
FT REGION 412 417 Substrate binding (By similarity).
FT ACT_SITE 518 518 By similarity.
FT METAL 538 538 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 540 540 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 543 543 Magnesium; via carbonyl oxygen (By
FT similarity).
FT BINDING 312 312 Coenzyme A (By similarity).
FT BINDING 388 388 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 501 501 Substrate (By similarity).
FT BINDING 516 516 Substrate (By similarity).
FT BINDING 524 524 Coenzyme A (By similarity).
FT BINDING 527 527 Substrate (By similarity).
FT BINDING 585 585 Coenzyme A.
FT MOD_RES 610 610 N6-acetyllysine (By similarity).
SQ SEQUENCE 651 AA; 71045 MW; 3A04CFD3ED436EC5 CRC64;
MSNESLANLL KEERRFAPPA DLAANANVTA EAYEQAKADR LGFWAEQARR LTWAKEPTET
LDWSNPPFAK WFKDGTLNVA YNCVDRHVEA GNGDRVAIHF EGESGDSRAL TYAQLKDEVS
KAANALLELG VQKGDRVAIY MPMIPETAIA MLACARIGAA HSVVFGGFSS DALATRIQDA
DARVVITADG GYRRGKPSAL KPAVDEAVER AGIVEHVLVV RRTGQDVAWD DSRDKWWHET
VDGQSAEHTP EAFDAEHPLF ILYTSGTTGK PKGILHTSGG YLTQTAYTHW AVFDLKPETD
VFWCTADVGW VTGHSYIVYG PLANGATQVM YEGTPDTPHQ GRFWEIVQKY GVTILYTAPT
AIRTFMKWGD DIPAKFDLSS LRVLGSVGEP INPEAWIWYR KNIGADATPV VDTWWQTETG
AMMITPLPGV THAKPGSAQR PLPGISATVV DDEANEVPNG GGGYLVLTEP WPSMLRTIWG
DDQRFIDTYW SRFEGKYFAG DGAKKDDDGD IWLLGRVDDV MLVSGHNIST TEVESALVSH
PSVAEAAVVG ATDETTGQAI VAFVILRGTT AESEDLVAEL RNHVGATLGP IAKPKRILPV
SELPKTRSGK IMRRLLRDVA ENRQVGDVTT LADSTVMDLI QTKLPAAPSE D
//
