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Acetyl-coenzyme A synthetase (AcCoA synthetase) (Acs) (EC 6.2.1.1) (Acetate--CoA ligase) (Acyl-activating enzyme)

 ACSA_MYCTU              Reviewed;         651 AA.
P9WQD1; L0TGD8; O69635;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
07-NOV-2018, entry version 26.
RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
Short=AcCoA synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
Short=Acs {ECO:0000255|HAMAP-Rule:MF_01123};
EC=6.2.1.1 {ECO:0000255|HAMAP-Rule:MF_01123};
AltName: Full=Acetate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_01123};
AltName: Full=Acyl-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01123};
Name=acsA {ECO:0000255|HAMAP-Rule:MF_01123}; Synonyms=acs;
OrderedLocusNames=Rv3667; ORFNames=MTV025.015;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
FUNCTION, AUTOACETYLATION AT LYS-617, MUTAGENESIS OF LYS-617,
BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
PubMed=21896569; DOI=10.1093/abbs/gmr076;
Li R., Gu J., Chen P., Zhang Z., Deng J., Zhang X.;
"Purification and characterization of the acetyl-CoA synthetase from
Mycobacterium tuberculosis.";
Acta Biochim. Biophys. Sin. 43:891-899(2011).
[3]
FUNCTION, ACETYLATION AT LYS-617, AND MUTAGENESIS OF LYS-617.
PubMed=21627103; DOI=10.1021/bi200156t;
Xu H., Hegde S.S., Blanchard J.S.;
"Reversible acetylation and inactivation of Mycobacterium tuberculosis
acetyl-CoA synthetase is dependent on cAMP.";
Biochemistry 50:5883-5892(2011).
[4]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
-!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA
(AcCoA), an essential intermediate at the junction of anabolic and
catabolic pathways. AcsA undergoes a two-step reaction. In the
first half reaction, AcsA combines acetate with ATP to form
acetyl-adenylate (AcAMP) intermediate. In the second half
reaction, it can then transfer the acetyl group from AcAMP to the
sulfhydryl group of CoA, forming the product AcCoA. M.tuberculosis
may use AcsA for both acetate and propionate assimilation.
{ECO:0000255|HAMAP-Rule:MF_01123, ECO:0000269|PubMed:21627103,
ECO:0000269|PubMed:21896569}.
-!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
acetyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01123}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01123,
ECO:0000269|PubMed:21896569};
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|HAMAP-Rule:MF_01123,
ECO:0000269|PubMed:21896569};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|HAMAP-Rule:MF_01123,
ECO:0000269|PubMed:21896569};
Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
Evidence={ECO:0000255|HAMAP-Rule:MF_01123,
ECO:0000269|PubMed:21896569};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_01123,
ECO:0000269|PubMed:21896569};
Note=Magnesium, but can also use calcium, manganese, nickel or
zinc ions. {ECO:0000255|HAMAP-Rule:MF_01123,
ECO:0000269|PubMed:21896569};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.35 mM for CoA (at pH 8 and at 37 degrees Celsius)
{ECO:0000269|PubMed:21896569};
KM=1.2 mM for acetate (at pH 8 and at 37 degrees Celsius)
{ECO:0000269|PubMed:21896569};
KM=2.1 mM for propionate (at pH 8 and at 37 degrees Celsius)
{ECO:0000269|PubMed:21896569};
KM=5.6 mM for ATP (at pH 8 and at 37 degrees Celsius)
{ECO:0000269|PubMed:21896569};
KM=509 mM for butyrate (at pH 8 and at 37 degrees Celsius)
{ECO:0000269|PubMed:21896569};
pH dependence:
Optimum pH is around 8. The enzyme is stable under neutral and
alkaline conditions, while its activity decreases rapidly below
pH 6.0. {ECO:0000269|PubMed:21896569};
Temperature dependence:
Optimum temperature is 37 degrees Celsius. It lost its activity
rapidly below 25 degrees Celsius or above 45 degrees Celsius.
{ECO:0000269|PubMed:21896569};
-!- PTM: Acetylated on Lys-617 by Pat in the presence of acetyl-CoA as
an acetyl donor and ATP. Acetylation results in the inactivation
of the enzyme. Deacetylation by the SIR2-homolog deacetylase CobB
is required to activate the enzyme. {ECO:0000269|PubMed:21627103}.
-!- MISCELLANEOUS: Could be also autoacetylated on Lys-617 in the
presence of acetate as an acetyl donor and ATP. Autoacetylation is
effectively inhibited by CoA. If CoA is not available or the
concentration of CoA is low in vivo, the enzyme can transfer
acetyl group from AcAMP to itself, resulting in autoacetylation
and inactivation. When CoA is available, the acetyl group is
donated to CoA forming AcCoA (PubMed:21896569).
{ECO:0000305|PubMed:21896569}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000255|HAMAP-Rule:MF_01123}.
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EMBL; AL123456; CCP46490.1; -; Genomic_DNA.
PIR; D70789; D70789.
RefSeq; NP_218184.1; NC_000962.3.
RefSeq; WP_003899631.1; NZ_NVQJ01000028.1.
ProteinModelPortal; P9WQD1; -.
SMR; P9WQD1; -.
STRING; 83332.Rv3667; -.
iPTMnet; P9WQD1; -.
PaxDb; P9WQD1; -.
EnsemblBacteria; CCP46490; CCP46490; Rv3667.
GeneID; 885479; -.
KEGG; mtu:Rv3667; -.
TubercuList; Rv3667; -.
eggNOG; ENOG4108IQF; Bacteria.
eggNOG; COG0365; LUCA.
KO; K01895; -.
OMA; DHWWHDL; -.
PhylomeDB; P9WQD1; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; HDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-UniRule.
GO; GO:0016208; F:AMP binding; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
CDD; cd05966; ACS; 1.
HAMAP; MF_01123; Ac_CoA_synth; 1.
InterPro; IPR011904; Ac_CoA_lig.
InterPro; IPR032387; ACAS_N.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
Pfam; PF16177; ACAS_N; 1.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome; Ligase; Magnesium;
Metal-binding; Nucleotide-binding; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:21969609}.
CHAIN 2 651 Acetyl-coenzyme A synthetase.
/FTId=PRO_0000208369.
NP_BIND 387 389 ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
NP_BIND 411 416 ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
REGION 190 193 Coenzyme A binding. {ECO:0000255|HAMAP-
Rule:MF_01123}.
METAL 545 545 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01123}.
METAL 547 547 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01123}.
METAL 550 550 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01123}.
BINDING 311 311 Coenzyme A. {ECO:0000255|HAMAP-
Rule:MF_01123}.
BINDING 508 508 ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
BINDING 523 523 ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
BINDING 531 531 Coenzyme A; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01123}.
BINDING 534 534 ATP. {ECO:0000255|HAMAP-Rule:MF_01123}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:21969609}.
MOD_RES 617 617 N6-acetyllysine. {ECO:0000255|HAMAP-
Rule:MF_01123,
ECO:0000269|PubMed:21627103}.
MUTAGEN 617 617 K->R: Complete loss of acetyl-coenzyme A
synthetase activity.
{ECO:0000269|PubMed:21627103,
ECO:0000269|PubMed:21896569}.
SEQUENCE 651 AA; 71476 MW; 94290C0517A0445B CRC64;
MSESTPEVSS SYPPPAHFAE HANARAELYR EAEEDRLAFW AKQANRLSWT TPFTEVLDWS
GAPFAKWFVG GELNVAYNCV DRHVEAGHGD RVAIHWEGEP VGDRRTLTYS DLLAEVSKAA
NALTDLGLVA GDRVAIYLPL IPEAVIAMLA CARLGIMHSV VFGGFTAAAL QARIVDAQAK
LLITADGQFR RGKPSPLKAA ADEALAAIPD CSVEHVLVVR RTGIEMAWSE GRDLWWHHVV
GSASPAHTPE PFDSEHPLFL LYTSGTTGKP KGIMHTSGGY LTQCCYTMRT IFDVKPDSDV
FWCTADIGWV TGHTYGVYGP LCNGVTEVLY EGTPDTPDRH RHFQIIEKYG VTIYYTAPTL
IRMFMKWGRE IPDSHDLSSL RLLGSVGEPI NPEAWRWYRD VIGGGRTPLV DTWWQTETGS
AMISPLPGIA AAKPGSAMTP LPGISAKIVD DHGDPLPPHT EGAQHVTGYL VLDQPWPSML
RGIWGDPARY WHSYWSKFSD KGYYFAGDGA RIDPDGAIWV LGRIDDVMNV SGHRISTAEV
ESALVAHSGV AEAAVVGVTD ETTTQAICAF VVLRANYAPH DRTAEELRTE VARVISPIAR
PRDVHVVPEL PKTRSGKIMR RLLRDVAENR ELGDTSTLLD PTVFDAIRAA K


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