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

 ACSA_SALTY              Reviewed;         652 AA.
Q8ZKF6;
26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
25-OCT-2017, entry version 98.
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=acs {ECO:0000255|HAMAP-Rule:MF_01123}; OrderedLocusNames=STM4275;
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=99287;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
PubMed=11677609; DOI=10.1038/35101614;
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium
LT2.";
Nature 413:852-856(2001).
[2]
ACETYLATION AT LYS-609, DEACETYLATION BY SIR2 HOMOLOG, AND MASS
SPECTROMETRY.
STRAIN=LT2 / SGSC1412 / ATCC 700720;
PubMed=12493915; DOI=10.1126/science.1077650;
Starai V.J., Celic I., Cole R.N., Boeke J.D., Escalante-Semerena J.C.;
"Sir2-dependent activation of acetyl-CoA synthetase by deacetylation
of active lysine.";
Science 298:2390-2392(2002).
[3]
ACETYLATION AT LYS-609.
STRAIN=LT2;
PubMed=15236963; DOI=10.1016/j.jmb.2004.05.010;
Starai V.J., Escalante-Semerena J.C.;
"Identification of the protein acetyltransferase (Pat) enzyme that
acetylates acetyl-CoA synthetase in Salmonella enterica.";
J. Mol. Biol. 340:1005-1012(2004).
[4]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND
COENZYME A, AND SUBUNIT.
PubMed=12627952; DOI=10.1021/bi0271603;
Gulick A.M., Starai V.J., Horswill A.R., Homick K.M.,
Escalante-Semerena J.C.;
"The 1.75 A crystal structure of acetyl-CoA synthetase bound to
adenosine-5'-propylphosphate and coenzyme A.";
Biochemistry 42:2866-2873(2003).
[5]
X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF WILD-TYPE AND MUTANTS IN
COMPLEX WITH THE ATP ANALOG AMP; COENZYME A AND MAGNESIUM IONS,
FUNCTION, MUTAGENESIS OF ARG-194; ALA-357; ASP-517; GLY-524; ARG-526;
ARG-584 AND LYS-609, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=17497934; DOI=10.1021/bi6026506;
Reger A.S., Carney J.M., Gulick A.M.;
"Biochemical and crystallographic analysis of substrate binding and
conformational changes in acetyl-CoA synthetase.";
Biochemistry 46:6536-6546(2007).
-!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA
(AcCoA), an essential intermediate at the junction of anabolic and
catabolic pathways. Acs undergoes a two-step reaction. In the
first half reaction, Acs 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. {ECO:0000255|HAMAP-
Rule:MF_01123, ECO:0000269|PubMed:17497934}.
-!- FUNCTION: Enables the cell to use acetate during aerobic growth to
generate energy via the TCA cycle, and biosynthetic compounds via
the glyoxylate shunt. Acetylates CheY, the response regulator
involved in flagellar movement and chemotaxis. {ECO:0000255|HAMAP-
Rule:MF_01123}.
-!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
acetyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01123}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=77.1 uM for ATP (at pH 7.5 and at 37 degrees Celsius)
{ECO:0000269|PubMed:17497934};
KM=50 uM for CoA (at pH 7.5 and at 37 degrees Celsius)
{ECO:0000269|PubMed:17497934};
KM=6047 uM for acetate (at pH 7.5 and at 37 degrees Celsius)
{ECO:0000269|PubMed:17497934};
KM=9413 uM for propionate (at pH 7.5 and at 37 degrees Celsius)
{ECO:0000269|PubMed:17497934};
KM=9450 uM for glycine (at pH 7.5 and at 37 degrees Celsius)
{ECO:0000269|PubMed:17497934};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12627952,
ECO:0000269|PubMed:17497934}.
-!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
activates the enzyme. {ECO:0000255|HAMAP-Rule:MF_01123,
ECO:0000269|PubMed:12493915, ECO:0000269|PubMed:15236963}.
-!- MASS SPECTROMETRY: Mass=733.4; Method=MALDI; Range=607-612;
Evidence={ECO:0000269|PubMed:12493915};
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000255|HAMAP-Rule:MF_01123}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AE006468; AAL23099.1; -; Genomic_DNA.
RefSeq; NP_463140.1; NC_003197.2.
RefSeq; WP_000083882.1; NC_003197.2.
PDB; 1PG3; X-ray; 2.30 A; A/B=1-652.
PDB; 1PG4; X-ray; 1.75 A; A/B=1-652.
PDB; 2P20; X-ray; 2.22 A; A/B=1-652.
PDB; 2P2B; X-ray; 2.20 A; A/B=1-652.
PDB; 2P2F; X-ray; 2.58 A; A/B=1-652.
PDB; 2P2J; X-ray; 2.30 A; A/B=1-652.
PDB; 2P2M; X-ray; 2.11 A; A/B=1-652.
PDB; 2P2Q; X-ray; 2.42 A; A/B=1-652.
PDB; 5JRH; X-ray; 1.64 A; A/B=1-652.
PDBsum; 1PG3; -.
PDBsum; 1PG4; -.
PDBsum; 2P20; -.
PDBsum; 2P2B; -.
PDBsum; 2P2F; -.
PDBsum; 2P2J; -.
PDBsum; 2P2M; -.
PDBsum; 2P2Q; -.
PDBsum; 5JRH; -.
ProteinModelPortal; Q8ZKF6; -.
SMR; Q8ZKF6; -.
STRING; 99287.STM4275; -.
DrugBank; DB03230; Adenosine-5'-Propylphosphate.
DrugBank; DB01992; Coenzyme A.
iPTMnet; Q8ZKF6; -.
PaxDb; Q8ZKF6; -.
PRIDE; Q8ZKF6; -.
EnsemblBacteria; AAL23099; AAL23099; STM4275.
GeneID; 1255801; -.
KEGG; stm:STM4275; -.
PATRIC; fig|99287.12.peg.4496; -.
eggNOG; ENOG4108IQF; Bacteria.
eggNOG; COG0365; LUCA.
HOGENOM; HOG000229981; -.
KO; K01895; -.
OMA; DHWWHDL; -.
PhylomeDB; Q8ZKF6; -.
EvolutionaryTrace; Q8ZKF6; -.
Proteomes; UP000001014; Chromosome.
GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
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;
3D-structure; Acetylation; ATP-binding; Complete proteome; Ligase;
Magnesium; Metal-binding; Nucleotide-binding; Reference proteome.
CHAIN 1 652 Acetyl-coenzyme A synthetase.
/FTId=PRO_0000208386.
NP_BIND 387 389 ATP.
NP_BIND 411 416 ATP.
REGION 191 194 Coenzyme A binding.
METAL 537 537 Magnesium; via carbonyl oxygen.
METAL 539 539 Magnesium; via carbonyl oxygen.
METAL 542 542 Magnesium; via carbonyl oxygen.
BINDING 311 311 Coenzyme A. {ECO:0000255|HAMAP-
Rule:MF_01123,
ECO:0000269|PubMed:12627952,
ECO:0000269|PubMed:17497934}.
BINDING 335 335 Coenzyme A. {ECO:0000255|HAMAP-
Rule:MF_01123,
ECO:0000269|PubMed:12627952,
ECO:0000269|PubMed:17497934}.
BINDING 500 500 ATP.
BINDING 515 515 ATP.
BINDING 523 523 Coenzyme A; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01123,
ECO:0000269|PubMed:12627952,
ECO:0000269|PubMed:17497934}.
BINDING 526 526 ATP.
BINDING 584 584 Coenzyme A. {ECO:0000255|HAMAP-
Rule:MF_01123,
ECO:0000269|PubMed:12627952,
ECO:0000269|PubMed:17497934}.
SITE 517 517 Hinge residue important for
conformational flexibility.
MOD_RES 609 609 N6-acetyllysine; by Pat.
{ECO:0000255|HAMAP-Rule:MF_01123,
ECO:0000269|PubMed:12493915,
ECO:0000269|PubMed:15236963}.
MUTAGEN 194 194 R->A: Results in a 2-fold reduction in
the catalytic efficiency for both ATP and
CoA. 2-fold increase in the affinity for
ATP and 3-fold reduction for CoA.
{ECO:0000269|PubMed:17497934}.
MUTAGEN 194 194 R->E: Results in a 2-fold reduction in
the catalytic efficiency for both ATP and
CoA. 2-fold increase in the affinity for
ATP and 2-fold reduction for CoA.
{ECO:0000269|PubMed:17497934}.
MUTAGEN 357 357 A->V: Results in a 2-fold reduction in
the catalytic efficiency for both ATP and
CoA. 3-fold increase in the affinity for
ATP and 3-fold reduction for CoA.
{ECO:0000269|PubMed:17497934}.
MUTAGEN 517 517 D->G: Results in a 2-fold reduction in
the catalytic efficiency for both ATP and
CoA. 2-fold increase in the affinity for
ATP and 10-fold reduction for CoA.
{ECO:0000269|PubMed:17497934}.
MUTAGEN 517 517 D->P: Results in a 2-fold reduction in
the catalytic efficiency for both ATP and
CoA. 3-fold reduction in the affinity for
ATP and 4.5-fold reduction for CoA.
{ECO:0000269|PubMed:17497934}.
MUTAGEN 524 524 G->L: No acetyl-coenzyme A synthetase
activity. {ECO:0000269|PubMed:17497934}.
MUTAGEN 524 524 G->S: Results in a 2-fold reduction in
the catalytic efficiency for both ATP and
CoA. Almost the same affinity as the
wild-type for ATP, but 9-fold reduction
in the affinity for CoA.
{ECO:0000269|PubMed:17497934}.
MUTAGEN 526 526 R->A: Results in a 2-fold reduction in
the catalytic efficiency for both ATP and
CoA. 3-fold increase in the affinity for
ATP and 4-fold reduction for CoA.
{ECO:0000269|PubMed:17497934}.
MUTAGEN 584 584 R->A: Results in a 2-fold reduction in
the catalytic efficiency for both ATP and
CoA. 2-fold increase in the affinity for
ATP and 7-fold reduction for CoA.
{ECO:0000269|PubMed:17497934}.
MUTAGEN 584 584 R->E: Results in a 2-fold reduction in
the catalytic efficiency for both ATP and
CoA. 3-fold increase in the affinity for
ATP and 8-fold reduction for CoA.
{ECO:0000269|PubMed:17497934}.
MUTAGEN 609 609 K->A: No acetyl-coenzyme A synthetase
activity. {ECO:0000269|PubMed:17497934}.
HELIX 11 16 {ECO:0000244|PDB:5JRH}.
HELIX 21 33 {ECO:0000244|PDB:5JRH}.
HELIX 35 42 {ECO:0000244|PDB:5JRH}.
HELIX 43 45 {ECO:0000244|PDB:5JRH}.
STRAND 56 59 {ECO:0000244|PDB:5JRH}.
STRAND 66 70 {ECO:0000244|PDB:5JRH}.
HELIX 77 81 {ECO:0000244|PDB:5JRH}.
HELIX 83 85 {ECO:0000244|PDB:5JRH}.
HELIX 86 89 {ECO:0000244|PDB:5JRH}.
STRAND 92 98 {ECO:0000244|PDB:5JRH}.
STRAND 105 109 {ECO:0000244|PDB:5JRH}.
HELIX 110 126 {ECO:0000244|PDB:5JRH}.
STRAND 134 138 {ECO:0000244|PDB:5JRH}.
HELIX 143 155 {ECO:0000244|PDB:5JRH}.
STRAND 158 161 {ECO:0000244|PDB:5JRH}.
HELIX 168 178 {ECO:0000244|PDB:5JRH}.
STRAND 181 187 {ECO:0000244|PDB:5JRH}.
STRAND 189 191 {ECO:0000244|PDB:5JRH}.
STRAND 194 196 {ECO:0000244|PDB:5JRH}.
HELIX 198 206 {ECO:0000244|PDB:5JRH}.
STRAND 216 220 {ECO:0000244|PDB:5JRH}.
TURN 231 233 {ECO:0000244|PDB:5JRH}.
STRAND 234 236 {ECO:0000244|PDB:5JRH}.
HELIX 237 243 {ECO:0000244|PDB:5JRH}.
STRAND 257 264 {ECO:0000244|PDB:5JRH}.
STRAND 267 270 {ECO:0000244|PDB:5JRH}.
STRAND 272 278 {ECO:0000244|PDB:5JRH}.
HELIX 279 292 {ECO:0000244|PDB:5JRH}.
STRAND 300 303 {ECO:0000244|PDB:5JRH}.
HELIX 310 314 {ECO:0000244|PDB:5JRH}.
TURN 315 317 {ECO:0000244|PDB:5JRH}.
HELIX 318 322 {ECO:0000244|PDB:5JRH}.
STRAND 326 330 {ECO:0000244|PDB:5JRH}.
STRAND 336 338 {ECO:0000244|PDB:5JRH}.
HELIX 341 349 {ECO:0000244|PDB:5JRH}.
STRAND 352 356 {ECO:0000244|PDB:5JRH}.
HELIX 358 365 {ECO:0000244|PDB:5JRH}.
HELIX 366 371 {ECO:0000244|PDB:5JRH}.
TURN 372 374 {ECO:0000244|PDB:5JRH}.
STRAND 382 388 {ECO:0000244|PDB:5JRH}.
HELIX 392 401 {ECO:0000244|PDB:5JRH}.
TURN 402 405 {ECO:0000244|PDB:5JRH}.
STRAND 409 413 {ECO:0000244|PDB:5JRH}.
HELIX 416 418 {ECO:0000244|PDB:5JRH}.
TURN 427 429 {ECO:0000244|PDB:5JRH}.
STRAND 438 440 {ECO:0000244|PDB:5JRH}.
STRAND 446 449 {ECO:0000244|PDB:5JRH}.
STRAND 458 466 {ECO:0000244|PDB:5JRH}.
HELIX 481 489 {ECO:0000244|PDB:5JRH}.
STRAND 490 492 {ECO:0000244|PDB:5JRH}.
STRAND 495 504 {ECO:0000244|PDB:5JRH}.
STRAND 510 522 {ECO:0000244|PDB:5JRH}.
STRAND 525 528 {ECO:0000244|PDB:5JRH}.
HELIX 529 537 {ECO:0000244|PDB:5JRH}.
STRAND 542 552 {ECO:0000244|PDB:5JRH}.
TURN 553 555 {ECO:0000244|PDB:5JRH}.
STRAND 556 565 {ECO:0000244|PDB:5JRH}.
HELIX 573 586 {ECO:0000244|PDB:5JRH}.
HELIX 589 591 {ECO:0000244|PDB:5JRH}.
STRAND 594 598 {ECO:0000244|PDB:5JRH}.
STRAND 604 607 {ECO:0000244|PDB:2P2M}.
HELIX 612 620 {ECO:0000244|PDB:5JRH}.
HELIX 629 631 {ECO:0000244|PDB:1PG4}.
STRAND 632 634 {ECO:0000244|PDB:2P2M}.
HELIX 637 646 {ECO:0000244|PDB:5JRH}.
SEQUENCE 652 AA; 72153 MW; 347209D1D3D349D8 CRC64;
MSQTHKHAIP ANIADRCLIN PEQYETKYKQ SINDPDTFWG EQGKILDWIT PYQKVKNTSF
APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD DTSQSKHISY RELHRDVCRF
ANTLLDLGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPEA VAGRIIDSSS
RLVITADEGV RAGRSIPLKK NVDDALKNPN VTSVEHVIVL KRTGSDIDWQ EGRDLWWRDL
IEKASPEHQP EAMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPGDI
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMCQVVDKHQ VNILYTAPTA
IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK KIGKEKCPVV DTWWQTETGG
FMITPLPGAI ELKAGSATRP FFGVQPALVD NEGHPQEGAT EGNLVITDSW PGQARTLFGD
HERFEQTYFS TFKNMYFSGD GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP
KIAEAAVVGI PHAIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM PS


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