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Acetyl-coenzyme A synthetase (AcCoA synthetase) (Acs) (EC 6.2.1.1) (Acetate--CoA ligase) (Acyl-activating enzyme)
A0A157U0Q1_ENTCL Unreviewed; 645 AA.
A0A157U0Q1;
08-JUN-2016, integrated into UniProtKB/TrEMBL.
08-JUN-2016, sequence version 1.
16-JAN-2019, entry version 11.
RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
Short=AcCoA synthetase {ECO:0000256|HAMAP-Rule:MF_01123};
Short=Acs {ECO:0000256|HAMAP-Rule:MF_01123};
EC=6.2.1.1 {ECO:0000256|HAMAP-Rule:MF_01123};
AltName: Full=Acetate--CoA ligase {ECO:0000256|HAMAP-Rule:MF_01123};
AltName: Full=Acyl-activating enzyme {ECO:0000256|HAMAP-Rule:MF_01123};
Name=acsA_1 {ECO:0000313|EMBL:SAI99703.1};
Synonyms=acs {ECO:0000256|HAMAP-Rule:MF_01123};
ORFNames=SAMEA2273162_00840 {ECO:0000313|EMBL:SAI99703.1};
Enterobacter cloacae.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
NCBI_TaxID=550 {ECO:0000313|EMBL:SAI99703.1, ECO:0000313|Proteomes:UP000249511};
[1] {ECO:0000313|EMBL:SAI99703.1, ECO:0000313|Proteomes:UP000249511}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=e403 {ECO:0000313|Proteomes:UP000249511};
Pathogen Informatics;
Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
-!- 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:0000256|HAMAP-
Rule:MF_01123}.
-!- 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.
{ECO:0000256|SAAS:SAAS00711888}.
-!- 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:0000256|HAMAP-
Rule:MF_01123}.
-!- CATALYTIC ACTIVITY:
Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
ChEBI:CHEBI:456215; EC=6.2.1.1; Evidence={ECO:0000256|HAMAP-
Rule:MF_01123};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01123,
ECO:0000256|SAAS:SAAS00711884};
-!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
activates the enzyme. {ECO:0000256|HAMAP-Rule:MF_01123}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000256|HAMAP-Rule:MF_01123}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01123}.
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EMBL; FKIY01000005; SAI99703.1; -; Genomic_DNA.
ProteinModelPortal; A0A157U0Q1; -.
Proteomes; UP000249511; Unassembled WGS sequence.
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:UniProtKB-UniRule.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
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.
3: Inferred from homology;
Acetylation {ECO:0000256|HAMAP-Rule:MF_01123};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01123};
Complete proteome {ECO:0000313|Proteomes:UP000249511};
Ligase {ECO:0000256|HAMAP-Rule:MF_01123, ECO:0000313|EMBL:SAI99703.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01123,
ECO:0000256|SAAS:SAAS00711869};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01123,
ECO:0000256|SAAS:SAAS00711886};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01123}.
DOMAIN 24 80 ACAS_N. {ECO:0000259|Pfam:PF16177}.
DOMAIN 82 519 AMP-binding. {ECO:0000259|Pfam:PF00501}.
DOMAIN 528 606 AMP-binding_C.
{ECO:0000259|Pfam:PF13193}.
NP_BIND 384 386 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
NP_BIND 408 413 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
REGION 190 193 Coenzyme A binding. {ECO:0000256|HAMAP-
Rule:MF_01123}.
METAL 534 534 Magnesium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01123}.
METAL 536 536 Magnesium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01123}.
METAL 539 539 Magnesium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01123}.
BINDING 308 308 Coenzyme A. {ECO:0000256|HAMAP-
Rule:MF_01123}.
BINDING 332 332 Coenzyme A. {ECO:0000256|HAMAP-
Rule:MF_01123}.
BINDING 497 497 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
BINDING 512 512 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
BINDING 520 520 Coenzyme A; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01123}.
BINDING 523 523 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
MOD_RES 606 606 N6-acetyllysine. {ECO:0000256|HAMAP-
Rule:MF_01123}.
SEQUENCE 645 AA; 71640 MW; D3F63891F880B1EA CRC64;
MFEISVHPVP DAVRQRAYLN DDDYQRLYRQ SVENPDEFWS EQAKAFLDWF KPWHSVHHGD
LRKGQATWFK GGQLNVAYNC IDRHLERRGE QIAIVWEGDN PSESAHITYR KLHHNVCRLA
NVLKSRGVEK GDRVCIYMPM IPEAAYAMLA CARIGAVHSV VFGGFSPDSL RDRILDADCR
TVITADEGVR GGKYIPLKQN VEKALKDCPD VSTVVVVERT QGDIPWVEGR DIWYHEALHA
ASADCPAEAM DAEDPLFILY TSGSTGKPKG VLHTTGGYLL GAAMTHKYVF DYHDGDVYWC
TADVGWVTGH SYIVYGPLAN GATTLMFEGV PNYPDASRFW QVIDKHQVNI FYTAPTAIRA
LMREGDAPVR QTSRSSLRLL GSVGEPINPE AWEWYYQVVG EKRCPIVDTW WQTETGSILI
TPLPGATALK PGSATRPFFG VQPVLLDEKG KEIDGAGSGV LAIKASWPSQ IRSVYGDHQR
MIDTYFKPYP GYYFSGDGAR RDEDGYYWIT GRVDDVINVS GHRIGTAEVE SALVLHDAVA
EAAVVGCPHD VKGQAIYAFV TLMAGSQPSE ALQQELLALV GKEIGSFAKP DHLQWAPSLP
KTRSGKIMRR ILRKIACNEL DSLGDTSTLA DPGVVQGLID NRLNR
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Pathways :
WP1577: amino acid conjugation of benzoic acid
WP1708: Terpenoid backbone biosynthesis
WP2199: Seed Development
WP521: amino acid conjugation of benzoic acid
WP2211: Geranylgeranyldiphosphate biosynthesis II (plastidic)
WP1097: Non-homologous end joining
WP1201: Non-homologous end joining
WP1208: Non-homologous end joining
WP1222: Non-homologous end joining
WP1242: Non-homologous end joining
WP1277: Non-homologous end joining
WP1324: Non-homologous end joining
WP142: mRNA processing
WP1493: Carbon assimilation C4 pathway
WP1570: Non-homologous end joining
WP1625: Base excision repair
WP1626: Benzoate degradation via CoA ligation
WP1634: Butanoate metabolism
WP1648: Fatty acid metabolism
WP1672: Mismatch repair
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair
WP1690: Propanoate metabolism
WP1695: Pyruvate metabolism
WP1706: Synthesis and degradation of ketone bodies
Related Genes :
Bibliography :
[24751484] Acetylation of acetyl-CoA synthetase from Mycobacterium tuberculosis leads to specific inactivation of the adenylation reaction.
[21896569] Purification and characterization of the acetyl-CoA synthetase from Mycobacterium tuberculosis.
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