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

 A0A069Q4Z2_PSEAI        Unreviewed;       651 AA.
A0A069Q4Z2;
01-OCT-2014, integrated into UniProtKB/TrEMBL.
01-OCT-2014, sequence version 1.
05-DEC-2018, entry version 47.
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=acsA1 {ECO:0000313|EMBL:CEI18086.1};
Synonyms=acs {ECO:0000313|EMBL:AVR84915.1},
acs_2 {ECO:0000313|EMBL:CRQ98028.1},
acsA {ECO:0000256|HAMAP-Rule:MF_01123};
ORFNames=C0043_06860 {ECO:0000313|EMBL:PXC08883.1},
C0044_06435 {ECO:0000313|EMBL:PXC02178.1},
C0046_05910 {ECO:0000313|EMBL:PXB94468.1},
C8257_24350 {ECO:0000313|EMBL:AVR84915.1},
CAZ10_11860 {ECO:0000313|EMBL:OTI62260.1},
CGU42_01775 {ECO:0000313|EMBL:OZO19386.1},
CW299_05975 {ECO:0000313|EMBL:PXB99133.1},
DI492_22670 {ECO:0000313|EMBL:PWH90037.1},
DN070_01560 {ECO:0000313|EMBL:RCH62253.1},
PAERUG_E15_London_28_01_14_07297 {ECO:0000313|EMBL:CRQ98028.1},
PAMH19_4224 {ECO:0000313|EMBL:CEI18086.1},
RW109_RW109_05301 {ECO:0000313|EMBL:SOV31173.1};
Pseudomonas aeruginosa.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=287 {ECO:0000313|EMBL:CEI18086.1, ECO:0000313|Proteomes:UP000043988};
[1] {ECO:0000313|EMBL:CEI18086.1, ECO:0000313|Proteomes:UP000043988}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MH19 {ECO:0000313|EMBL:CEI18086.1,
ECO:0000313|Proteomes:UP000043988};
Wibberg Daniel;
Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:CRQ98028.1}
NUCLEOTIDE SEQUENCE.
STRAIN=E15_London_28_01_14 {ECO:0000313|EMBL:CRQ98028.1};
Radhakrishnan Rajesh, Underwood Anthony, Al-Shahib Ali;
Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:OTI62260.1, ECO:0000313|Proteomes:UP000194857}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=S567_C10_BS {ECO:0000313|EMBL:OTI62260.1,
ECO:0000313|Proteomes:UP000194857};
Song R., Chenine A.L., Ruprecht R.M.;
Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:OZO19386.1, ECO:0000313|Proteomes:UP000216659}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ocean-1187 {ECO:0000313|EMBL:OZO19386.1,
ECO:0000313|Proteomes:UP000216659};
Kumagai Y., Yoshizawa S., Kogure K.;
"Genome sequencing of oceanic Pseudomonas aeruginosa.";
Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|EMBL:SOV31173.1, ECO:0000313|Proteomes:UP000233777}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RW109 {ECO:0000313|EMBL:SOV31173.1};
Hurst M.R.H.;
Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|EMBL:AVR84915.1, ECO:0000313|Proteomes:UP000241101}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MRSN12280 {ECO:0000313|EMBL:AVR84915.1,
ECO:0000313|Proteomes:UP000241101};
Snesrud E., Ong A.C., Kwak Y.I., Jones A.R., Hinkle M.K., Mc Gann P.;
"Sequencing of Colistin Resistant Pseudomonas aeruginosa.";
Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000313|EMBL:PWH90037.1, ECO:0000313|Proteomes:UP000245486}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PAL0.1 {ECO:0000313|EMBL:PWH90037.1,
ECO:0000313|Proteomes:UP000245486};
Grandjean T., Le Guern R., Bauduin M., Dessein R., Kipnis E.,
Faure K., Duployez C.;
"In vivo anti-infectious effect of lectins inhibitors.";
Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000313|Proteomes:UP000246712, ECO:0000313|Proteomes:UP000246728, ECO:0000313|Proteomes:UP000247072}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LIM1303 {ECO:0000313|EMBL:PXC08883.1},
LIM1410 {ECO:0000313|EMBL:PXC02178.1,
ECO:0000313|Proteomes:UP000247072},
LIM1680 {ECO:0000313|EMBL:PXB94468.1,
ECO:0000313|Proteomes:UP000246728}, and
LIM4285 {ECO:0000313|EMBL:PXB99133.1,
ECO:0000313|Proteomes:UP000246712};
Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M.,
Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Rusch D.,
Podicherti R., Tsui H.-C.T., Winkler M.E.;
Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
[9] {ECO:0000313|Proteomes:UP000246712, ECO:0000313|Proteomes:UP000246728, ECO:0000313|Proteomes:UP000247072}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LIM1303 {ECO:0000313|EMBL:PXC08883.1},
LIM1410 {ECO:0000313|EMBL:PXC02178.1,
ECO:0000313|Proteomes:UP000247072},
LIM1680 {ECO:0000313|EMBL:PXB94468.1,
ECO:0000313|Proteomes:UP000246728}, and
LIM4285 {ECO:0000313|EMBL:PXB99133.1,
ECO:0000313|Proteomes:UP000246712};
Martins R.C.R., Perdigao-Neto L.V., Costa S.F., Levin A.S.S.;
"Pseudomonas aeruginosa genome sequencing and assembly.";
Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
[10] {ECO:0000313|EMBL:RCH62253.1, ECO:0000313|Proteomes:UP000252818}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TUEPA7472 {ECO:0000313|EMBL:RCH62253.1,
ECO:0000313|Proteomes:UP000252818};
Miess H., Jahanshah G., Broetz-Oesterhelt H., Willmann M., Peter S.,
Gross H.;
"Draft Genome Sequence of the Extensively Drug-Resistant (XDR / 4MRGN)
Pseudomonas aeruginosa Clinical Isolate TUEPA7472.";
Submitted (JUL-2018) 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. 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|HAMAP-Rule:MF_01123, ECO:0000256|SAAS:SAAS00711888}.
-!- 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}.
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EMBL; CP028162; AVR84915.1; -; Genomic_DNA.
EMBL; CDAZ01000013; CEI18086.1; -; Genomic_DNA.
EMBL; CVWF01000363; CRQ98028.1; -; Genomic_DNA.
EMBL; NFFZ01000005; OTI62260.1; -; Genomic_DNA.
EMBL; NMRQ01000004; OZO19386.1; -; Genomic_DNA.
EMBL; QFRL01000020; PWH90037.1; -; Genomic_DNA.
EMBL; QHLW01000313; PXB94468.1; -; Genomic_DNA.
EMBL; QHLS01000351; PXB99133.1; -; Genomic_DNA.
EMBL; QHLU01000490; PXC02178.1; -; Genomic_DNA.
EMBL; QHLR01000600; PXC08883.1; -; Genomic_DNA.
EMBL; QOLE01000001; RCH62253.1; -; Genomic_DNA.
EMBL; LT969520; SOV31173.1; -; Genomic_DNA.
RefSeq; WP_003110260.1; NZ_UGUO01000001.1.
EnsemblBacteria; CEI18086; CEI18086; PAMH19_4224.
EnsemblBacteria; CRQ03533; CRQ03533; PAERUG_P32_London_17_VIM_2_10_11_06111.
EnsemblBacteria; CRQ98028; CRQ98028; PAERUG_E15_London_28_01_14_07297.
KEGG; paeb:NCGM1900_1835; -.
PATRIC; fig|287.1477.peg.5426; -.
eggNOG; ENOG4108IQF; Bacteria.
eggNOG; COG0365; LUCA.
KO; K01895; -.
Proteomes; UP000043988; Unassembled WGS sequence.
Proteomes; UP000194857; Unassembled WGS sequence.
Proteomes; UP000216659; Unassembled WGS sequence.
Proteomes; UP000233777; Chromosome mainomosome.
Proteomes; UP000241101; Chromosome.
Proteomes; UP000245486; Unassembled WGS sequence.
Proteomes; UP000246712; Unassembled WGS sequence.
Proteomes; UP000246728; Unassembled WGS sequence.
Proteomes; UP000247072; Unassembled WGS sequence.
Proteomes; UP000252818; 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: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.
3: Inferred from homology;
Acetylation {ECO:0000256|HAMAP-Rule:MF_01123};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01123};
Complete proteome {ECO:0000313|Proteomes:UP000043988,
ECO:0000313|Proteomes:UP000194857, ECO:0000313|Proteomes:UP000216659,
ECO:0000313|Proteomes:UP000233777};
Ligase {ECO:0000256|HAMAP-Rule:MF_01123, ECO:0000313|EMBL:CEI18086.1};
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 81 ACAS_N. {ECO:0000259|Pfam:PF16177}.
DOMAIN 83 522 AMP-binding. {ECO:0000259|Pfam:PF00501}.
DOMAIN 531 609 AMP-binding_C.
{ECO:0000259|Pfam:PF13193}.
NP_BIND 387 389 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
NP_BIND 411 416 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
REGION 191 194 Coenzyme A binding. {ECO:0000256|HAMAP-
Rule:MF_01123}.
METAL 537 537 Magnesium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01123}.
METAL 539 539 Magnesium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01123}.
METAL 542 542 Magnesium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01123}.
BINDING 311 311 Coenzyme A. {ECO:0000256|HAMAP-
Rule:MF_01123}.
BINDING 335 335 Coenzyme A. {ECO:0000256|HAMAP-
Rule:MF_01123}.
BINDING 500 500 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
BINDING 515 515 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
BINDING 523 523 Coenzyme A; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01123}.
BINDING 526 526 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
BINDING 584 584 Coenzyme A. {ECO:0000256|HAMAP-
Rule:MF_01123}.
MOD_RES 609 609 N6-acetyllysine. {ECO:0000256|HAMAP-
Rule:MF_01123}.
SEQUENCE 651 AA; 71763 MW; 991802723539AD23 CRC64;
MSAASLYPVH PEAVARTFTD EATYKTMYQQ SVVNPDGFWR EQAQRIDWIK PFEKVKQTSF
DDHHVDIKWF ADGTLNVSHN CLDRHLAERG DQVAIIWEGD DPADHQEITY RQLHEQVCKF
ANALRGQDVH RGDVVTIYMP MIPEAVVAML ACTRIGAIHS VVFGGFSPEA LAGRIIDCKS
KVVITADEGV RGGKRTPLKA NVDDALTNPE TSSVQKIIVC KRTGAEIKWN QHRDVWYDDL
MKVAGSTCAP KEMGAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYASLTHE RVFDYRPGEV
YWCTADIGWV TGHTYIVYGP LANGATTILF EGVPNYPDVT RVAKIIDKHK VNILYTAPTA
IRAMMAEGKA AVAGADGSSL RLLGSVGEPI NPEAWQWYYE TVGQSRCPIV DTWWQTETGA
CLMTPLPGAH AMKPGSAAKP FFGVVPALVD NLGNLIEGAA EGNLVILDSW PGQARTLFGD
HDRFVDTYFK TFKGMYFTGD GARRDEDGYY WITGRVDDVL NVSGHRMGTA EVESAMVAHP
KVAEAAVVGM QHDIKGQGIY VYVTLNSGVE PSEALRQELK QWVRREIGPI ATPDVIQWAP
GLPKTRSGKI MRRILRKIAA AEYDTLGDIS TLADPGVVQH LIETHRSMQA A


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