[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=DSM 1825 / TM-1; PubMed=8226623 [NCBI, ExPASy, EBI, Israel, Japan] Latimer M.T., Ferry J.G.; "Cloning, sequence analysis, and hyperexpression of the genes encoding phosphotransacetylase and acetate kinase from Methanosarcina thermophila."; J. Bacteriol. 175:6822-6829(1993).
[2]	PROTEIN SEQUENCE OF 1-17. PubMed=2844814 [NCBI, ExPASy, EBI, Israel, Japan] Aceti D.J., Ferry J.G.; "Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila. Evidence for regulation of synthesis."; J. Biol. Chem. 263:15444-15448(1988).
[3]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 9-408. DOI=10.1128/JB.183.2.680-686.2001; PubMed=11133963 [NCBI, ExPASy, EBI, Israel, Japan] Buss K.A., Cooper D.R., Ingram-Smith C., Ferry J.G., Sanders D.A., Hasson M.S.; "Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases."; J. Bacteriol. 183:680-686(2001).

Comments

CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate.
CATALYTIC ACTIVITY: ATP + propanoate = ADP + propanoyl phosphate.
ENZYME REGULATION: Inhibited by diethylpyrocarbonate and phenylglyoxal.
BIOPHYSICOCHEMICAL PROPERTIES:

Temperature dependence: Optimum temperature is 65 degrees Celsius. Protected from thermal inactivation by ATP;
PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2 .
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the acetokinase 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

L23147; AAA72042.1; -; Unassigned_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B49338; B49338.

3D structure databases

PDB

1G99; X-ray; 2.50 A; A/B=1-408.	[ExPASy / RCSB / EBI]
1TUU; X-ray; 2.50 A; A/B=1-399.	[ExPASy / RCSB / EBI]
1TUY; X-ray; 3.00 A; A/B=1-399.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1G99; -.
1TUU; -.
1TUY; -.

ModBase

P38502.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0008776;	Molecular function: acetate kinase activity (inferred from electronic annotation from HAMAP).
GO:0016310;	Biological process: phosphorylation (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00020; -; 1.
PBIL [Tree]

InterPro

IPR000890; Acetate_kin.
IPR004372; AckA.
Graphical view of domain structure.

PANTHER

PTHR21060; Acetate_kin; 1.
PTHR21060:SF11; AckA; 1.

Pfam

PF00871; Acetate_kinase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000722; Acetate_prop_kin; 1.

PRINTS

PR00471; ACETATEKNASE.

TIGRFAMs

TIGR00016; ackA; 1.

PROSITE

PS01075; ACETATE_KINASE_1; 1.
PS01076; ACETATE_KINASE_2; 1.

BLOCKS

P38502.

Other

DrugBank

DB00131; Adenosine monophosphate.

ProtoNet

P38502.

UniRef

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

Keywords

3D-structure; Cytoplasm; Direct protein sequencing; Kinase; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 408`	`408`	`Acetate kinase.`	`PRO_0000107650`
`STRAND`	`2 8`	`7`
`STRAND`	`13 19`	`7`
`TURN`	`20 23`	`4`
`STRAND`	`24 33`	`10`
`STRAND`	`36 38`	`3`
`STRAND`	`40 45`	`6`
`STRAND`	`50 54`	`5`
`HELIX`	`60 71`	`12`
`TURN`	`74 76`	`3`
`HELIX`	`82 84`	`3`
`STRAND`	`87 93`	`7`
`TURN`	`96 98`	`3`
`HELIX`	`107 115`	`9`
`HELIX`	`117 119`	`3`
`TURN`	`121 123`	`3`
`HELIX`	`124 137`	`14`
`STRAND`	`143 147`	`5`
`HELIX`	`150 154`	`5`
`HELIX`	`157 160`	`4`
`HELIX`	`166 172`	`7`
`HELIX`	`181 195`	`15`
`HELIX`	`199 201`	`3`
`STRAND`	`203 219`	`17`
`STRAND`	`222 227`	`6`
`STRAND`	`234 236`	`3`
`HELIX`	`249 257`	`9`
`HELIX`	`261 270`	`10`
`HELIX`	`273 278`	`6`
`HELIX`	`284 292`	`9`
`HELIX`	`296 319`	`24`
`STRAND`	`324 329`	`6`
`HELIX`	`330 335`	`6`
`HELIX`	`337 344`	`8`
`HELIX`	`348 350`	`3`
`HELIX`	`358 360`	`3`
`STRAND`	`374 379`	`6`
`HELIX`	`384 397`	`14`

Sequence information

Length: 408 AA [This is the length of the unprocessed precursor]

Molecular weight: 44337 Da [This is the MW of the unprocessed precursor]

CRC64: 1A484DF8A7258800 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKVLVINAGS SSLKYQLIDM TNESALAVGL CERIGIDNSI ITQKKFDGKK LEKLTDLPTH 

        70         80         90        100        110        120 
KDALEEVVKA LTDDEFGVIK DMGEINAVGH RVVHGGEKFT TSALYDEGVE KAIKDCFELA 

       130        140        150        160        170        180 
PLHNPPNMMG ISACAEIMPG TPMVIVFDTA FHQTMPPYAY MYALPYDLYE KHGVRKYGFH 

       190        200        210        220        230        240 
GTSHKYVAER AALMLGKPAE ETKIITCHLG NGSSITAVEG GKSVETSMGF TPLEGLAMGT 

       250        260        270        280        290        300 
RCGSIDPAIV PFLMEKEGLT TREIDTLMNK KSGVLGVSGL SNDFRDLDEA ASKGNRKAEL 

       310        320        330        340        350        360 
ALEIFAYKVK KFIGEYSAVL NGADAVVFTA GIGENSASIR KRILTGLDGI GIKIDDEKNK 

       370        380        390        400 
IRGQEIDIST PDAKVRVFVI PTNEELAIAR ETKEIVETEV KLRSSIPV

P38502 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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