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

 A0A1U2VZH3_9MYCO        Unreviewed;       658 AA.
A0A1U2VZH3;
10-MAY-2017, integrated into UniProtKB/TrEMBL.
10-MAY-2017, sequence version 1.
10-OCT-2018, entry version 10.
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=acs {ECO:0000313|EMBL:SKT80095.1};
Synonyms=acs_1 {ECO:0000313|EMBL:SKV17143.1},
acsA {ECO:0000256|HAMAP-Rule:MF_01123};
ORFNames=SAMEA2070716_04116 {ECO:0000313|EMBL:SKV17143.1},
SAMEA2275645_03690 {ECO:0000313|EMBL:SKM45198.1},
SAMEA2275744_02760 {ECO:0000313|EMBL:SKT80095.1},
SAMEA4008302_04691 {ECO:0000313|EMBL:SLB52709.1};
Mycobacteroides abscessus subsp. massiliense.
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacteroides; Mycobacteroides abscessus.
NCBI_TaxID=1962118 {ECO:0000313|EMBL:SKT80095.1, ECO:0000313|Proteomes:UP000190302};
[1] {ECO:0000313|Proteomes:UP000190302, ECO:0000313|Proteomes:UP000248866, ECO:0000313|Proteomes:UP000249573}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1018 {ECO:0000313|EMBL:SKT80095.1,
ECO:0000313|Proteomes:UP000190302}, 114 {ECO:0000313|EMBL:SKV17143.1,
ECO:0000313|Proteomes:UP000248866}, 923 {ECO:0000313|EMBL:SKM45198.1,
ECO:0000313|Proteomes:UP000249573},
Aerosol_16 {ECO:0000313|EMBL:SLB52709.1}, and
aerosol_16 {ECO:0000313|Proteomes:UP000249801};
Pathogen Informatics;
Submitted (NOV-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. 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}.
-!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
acetyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01123}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01123};
-!- 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; FVHE01000004; SKM45198.1; -; Genomic_DNA.
EMBL; FVMV01000005; SKT80095.1; -; Genomic_DNA.
EMBL; FVNU01000005; SKV17143.1; -; Genomic_DNA.
EMBL; FVSE01000004; SLB52709.1; -; Genomic_DNA.
RefSeq; WP_005063290.1; NZ_NREJ01000010.1.
Proteomes; UP000190302; Unassembled WGS sequence.
Proteomes; UP000248866; Unassembled WGS sequence.
Proteomes; UP000249573; Unassembled WGS sequence.
Proteomes; UP000249801; 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:UP000190302,
ECO:0000313|Proteomes:UP000248866, ECO:0000313|Proteomes:UP000249573,
ECO:0000313|Proteomes:UP000249801};
Ligase {ECO:0000256|HAMAP-Rule:MF_01123, ECO:0000313|EMBL:SKT80095.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01123};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01123};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01123}.
DOMAIN 26 78 ACAS_N. {ECO:0000259|Pfam:PF16177}.
DOMAIN 85 536 AMP-binding. {ECO:0000259|Pfam:PF00501}.
DOMAIN 545 624 AMP-binding_C.
{ECO:0000259|Pfam:PF13193}.
NP_BIND 394 396 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
NP_BIND 418 423 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
REGION 188 191 Coenzyme A binding. {ECO:0000256|HAMAP-
Rule:MF_01123}.
METAL 551 551 Magnesium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01123}.
METAL 553 553 Magnesium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01123}.
METAL 556 556 Magnesium; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01123}.
BINDING 318 318 Coenzyme A. {ECO:0000256|HAMAP-
Rule:MF_01123}.
BINDING 514 514 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
BINDING 529 529 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
BINDING 537 537 Coenzyme A; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01123}.
BINDING 540 540 ATP. {ECO:0000256|HAMAP-Rule:MF_01123}.
MOD_RES 624 624 N6-acetyllysine. {ECO:0000256|HAMAP-
Rule:MF_01123}.
SEQUENCE 658 AA; 72305 MW; 2559B1E9BCB3C415 CRC64;
MTETSIEPDS YPPSPEFVAT ANATADLYQA AEEDRLGFWE QQAGRLHWDE PFRQVLDWSD
APFAKWFVGG KLNVAYNCVD RHVEAGNGDR VAIHWEGEPG DTRTITYAEL LAKVSQAANY
LTELGLVSGD RVAIYMPMLP EAIVAMLACA RLGLMHSVVF AGFSAAALRA RIDDAQAKLV
ITSDGQWRRG TAAPLKSQVD EALGAAGPAT SDLGGEPSSV EHVLVVRRTE IPVEWTEGRD
LWWHETVDKA DTTHTAEPFD SEHPLFLLYT SGTTGKPKGI VHTSGGFLTQ TSYTHFNIFD
LKPETDVYWC TADIGWVTGH TYIVYGPLSN GATQVVYEGT PTSPNEHRHF EIIEKYGVTI
YYIAPTLVRT FMKWGREIPF AHDLSSLRLL GSVGEPINPE AWRWYREVIG GNRTPIVDTW
WQTETGSAMI SPLPGVTETK PGSAMRAVPG ISAKIVDDEG NQLEPASGDE PVTGYLVLDK
PWPSMLRGIW GDPERFKETY WSRYAEQGWY FAGDGARYDS DGAIWVLGRI DDVMNISGHR
ISTAEVESAL VGHDGVAEAA VVGASDETTG QAIVAFVILK ASHTVEGDEL VAHLKAQVSK
EISPIAKPRE IHVVPELPKT RSGKIMRRLL RDVAEGRELG DTSTLVDPSV FEAIRASK


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