[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Opfikon / DSM 2139; PubMed=1680850 [NCBI, ExPASy, EBI, Israel, Japan] Eggen R.I.L., Geerling A.C.M., Boshoven A.B.P., de Vos W.M.; "Cloning, sequence analysis, and functional expression of the acetyl coenzyme A synthetase gene from Methanothrix soehngenii in Escherichia coli."; J. Bacteriol. 173:6383-6389(1991).
[2]	CHARACTERIZATION. PubMed=2571608 [NCBI, ExPASy, EBI, Israel, Japan] Jetten M.S., Stams A.J., Zehnder A.J.; "Isolation and characterization of acetyl-coenzyme A synthetase from Methanothrix soehngenii."; J. Bacteriol. 171:5430-5435(1989).

Comments

CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
SUBUNIT: Homodimer.
PTM: The N-terminus is blocked.
PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme (By similarity).
SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M63968; AAA73007.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A41043; A41043.

3D structure databases

HSSP

Q8ZKF6; 1PG4. [HSSP ENTRY / PDB]

ModBase

P27095.

Ontologies

GO:0003987;	Molecular function: acetate-CoA ligase activity (inferred from electronic annotation from HAMAP).
GO:0016208;	Molecular function: AMP binding (inferred from electronic annotation from InterPro).
GO:0008152;	Biological process: metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_01123; -; 1.
PBIL [Tree]

InterPro

IPR011904; Ac_CoA_lig_AcsA.
IPR000873; AMP-dep_Synth/Lig.
Graphical view of domain structure.

Pfam

PF00501; AMP-binding; 1.
Pfam graphical view of domain structure.

PRINTS

PR00154; AMPBINDING.

TIGRFAMs

TIGR02188; Ac_CoA_lig_AcsA; 1.

PROSITE

PS00455; AMP_BINDING; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Ligase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 672`	`672`	`Acetyl-coenzyme A synthetase.`	`PRO_0000208401`
`ACT_SITE`	`546 546`		`By similarity.`
`MOD_RES`	`638 638`		`N6-acetyllysine (By similarity).`

Sequence information

Length: 672 AA [This is the length of the unprocessed precursor]

Molecular weight: 75527 Da [This is the MW of the unprocessed precursor]

CRC64: D3CB6AC88BAEAF65 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLKLAGKEDK KLKTTVFQDE TRIFNPPKEL VEKSIVMQWM KKKGFKTEKE MRAWCSSDEH 

        70         80         90        100        110        120 
YLEFWDEMAK TYVDWHKPYT KVMDDSEMPY FHWFTGGEIN ITYNAVDRHA KGAKKDKVAY 

       130        140        150        160        170        180 
IWIPEPTDQP VQKITYGDLY KEVNKFANGL KSLGLKKGDR VSIYMPMIPQ LPIAMLACAK 

       190        200        210        220        230        240 
LGVSHIVVFS GFSSKGLMDR AAHCGSRAII TVDGFYRRGK PVPLKPNADE AAGGAPSVEK 

       250        260        270        280        290        300 
IIVYKRAGVD VSMKEGRDVW WHDLVKGQSE ECEPVWVDPE HRLYILYTSG TTGKPKGIEH 

       310        320        330        340        350        360 
ATGGNAVGPA QTLHWVFDLK DDDVWWCTAD IGWVTGHSYI VYAPLILGMT SLMYEGAADY 

       370        380        390        400        410        420 
PDFGRWWKNI QDHKVTVLYT APTAVRMFMK QGAEWPDKYD LSSLRLLGSV GEPINPEAWM 

       430        440        450        460        470        480 
WYREHIGRGE LQIMDTWWQT ETGTFLNSPL PITPLKPGSC TFPLPGYDIS ILDEEGNEVP 

       490        500        510        520        530        540 
LGSGGNIVAL KPYPSMLRAF WGDKERFMKE YWQFYWDVPG RRGVYLAGDK AQRDKDGYFF 

       550        560        570        580        590        600 
IQGRIDDVLS VAGHRIANAE VESALVAHPK IAEAAVVGKP DEVKGESIVA FVILRVGNEP 

       610        620        630        640        650        660 
SPELAKDAIA FVRKTLGPVA APTEVHFVND LPKTRSGKIM RRVVKARALG NPVGDISTLM 

       670 
NPEAVDGIPK IV

P27095 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools