ID ACSA_LEPBL Reviewed; 654 AA.
AC Q056J9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 01-MAY-2013, entry version 47.
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=LBL_0125;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L550;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A.,
RA Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P.,
RA Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000348; ABJ77746.1; -; Genomic_DNA.
DR RefSeq; YP_796679.1; NC_008508.1.
DR ProteinModelPortal; Q056J9; -.
DR SMR; Q056J9; 10-650.
DR STRING; 355276.LBL_0125; -.
DR EnsemblBacteria; ABJ77746; ABJ77746; LBL_0125.
DR GeneID; 4408535; -.
DR KEGG; lbl:LBL_0125; -.
DR PATRIC; 22363334; VBILepBor75619_0146.
DR eggNOG; COG0365; -.
DR HOGENOM; HOG000229981; -.
DR KO; K01895; -.
DR OMA; HQRMVDT; -.
DR ProtClustDB; PRK00174; -.
DR BioCyc; LBOR355276:GHUQ-428-MONOMER; -.
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 1 654 Acetyl-coenzyme A synthetase.
FT /FTId=PRO_1000085002.
FT REGION 413 418 Substrate binding (By similarity).
FT ACT_SITE 521 521 By similarity.
FT METAL 541 541 Magnesium; via carbonyl oxygen (By
FT similarity).
FT METAL 546 546 Magnesium; via carbonyl oxygen (By
FT similarity).
FT BINDING 313 313 Coenzyme A (By similarity).
FT BINDING 389 389 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 504 504 Substrate (By similarity).
FT BINDING 519 519 Substrate (By similarity).
FT BINDING 527 527 Coenzyme A (By similarity).
FT BINDING 530 530 Substrate (By similarity).
FT BINDING 588 588 Coenzyme A.
FT MOD_RES 613 613 N6-acetyllysine (By similarity).
SQ SEQUENCE 654 AA; 73402 MW; 2A51CC717429B00A CRC64;
MAKERIVLPS AEFKKNSNIT LKDYKSLYKE SIENPNKFWA KEANRLTWFK KWTKVLNHDF
KNAKVEWFKG GKLNVSYNCL DRHISTPLKN KAALIWEGDN PSESKVLTYY DVYREVNRFA
NVLKKYGVKK GDRVLVYLPM IPELAITILA CTRIGAIHSV VFGGFSPEAL QSRIDDCKPK
LIVTADGGFR GGKPIELKRN VDIALEKSKE DVKTVIVVRR TGNESGLVWK DGRDYWYHFL
ISDPDLSPYC KPESMDAEDP LFILYTSGST GKPKGVLHTT GGYLLGVNLT FHYVFDIKPE
DTYWCTADIG WVTGHSYLVY GPLSNGASSV MFEGVPSYPD AGRFWDVIDK YGVNIFYTAP
TAIRALMREG LTHVQKRNLS SLRLLGSVGE PINPEAWEWY FKIIGKEKCP IVDTWWQTET
GSIMITALPG AIPQKPGSAT LPFFGVQPVL VDNDGKEIND KGEVSGNLCI KSPWPSMMRG
VYGDSKRFFD TYFSQFKGYY FTGDGARRDK DGYYWITGRV DDVINVSGHR IGSAEVESAL
VENRSVAEAA VVGFPHDIKG QGIYAYVTVK EGIATNDTLK KELVAIVEKV IGKIARPDVI
HWAPSLPKTR SGKIMRRILR KIASGEFEGL GDTSTLADPS VVQKLIEDKR KFHS
//
