Acetate kinase - Methanosarcina thermophila

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P38502 (ACKA_METTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acetate kinase
EC=2.7.2.1

Alternative name(s):
Acetokinase

Gene names

Name:	ackA
Synonyms:	ack

Organism

Methanosarcina thermophila

Taxonomic identifier

2210 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. Can also phosphorylate propionate, but has very low activity toward butyrate. Ref.4
Catalytic activity	ATP + acetate = ADP + acetyl phosphate. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7
Cofactor	Mg²⁺. Can also accept Mn²⁺. The Mg²⁺ is bound between two conserved protein residues and the ATP phosphate groups. Ref.3 Ref.7
Enzyme regulation	Inhibited by diethylpyrocarbonate, hydroxylamine and phenylglyoxal. Ref.1 Ref.7
Pathway	Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2. HAMAP-Rule MF_00020
Subunit structure	Homodimer. Ref.2 Ref.3 Ref.5 Ref.6 Ref.7
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the acetokinase family.
Biophysicochemical properties	Kinetic parameters: K_M=71 µM for ATP Ref.1 Ref.2 Ref.4 Ref.5 Ref.7 K_M=98 µM for ADP K_M=1.5 mM for acetate K_M=0.47 mM for acetyl phosphate Temperature dependence: Optimum temperature is 65 degrees Celsius. Protected from thermal inactivation by ATP.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway organic acid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate kinase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 408

408

Acetate kinase HAMAP-Rule MF_00020

PRO_0000107650

Regions

Nucleotide binding

208 – 212

ATP HAMAP-Rule MF_00020

Nucleotide binding

283 – 285

ATP HAMAP-Rule MF_00020

Nucleotide binding

331 – 335

ATP HAMAP-Rule MF_00020

Sites

Active site

148

Proton donor/acceptor Ref.6 Ref.7

Metal binding

Magnesium Probable

Metal binding

384

Magnesium Probable

Binding site

ATP

Binding site

Substrate

Site

180

Transition state stabilizer

Site

241

Transition state stabilizer

Experimental info

Mutagenesis

N → A: Almost abolishes catalytic activity. Requires increased magnesium levels for activity. Strongly decreases affinity for acetate. Ref.3

Mutagenesis

N → D: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Ref.3

Mutagenesis

S → A or T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate. Ref.3

Mutagenesis

S → A: Decreases catalytic activity. Decreases affinity for acetate.

Mutagenesis

S → T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate.

Mutagenesis

S → A: Decreases catalytic activity. Strongly decreases affinity for acetate. Requires increased magnesium levels for enzyme activity. Ref.3

Mutagenesis

S → T: Decreases catalytic activity. Strongly decreases affinity for acetate. Ref.3

Mutagenesis

K → A: Strongly decreases enzyme activity. Ref.3

Mutagenesis

K → R: Reduces enzyme activity. Ref.3

Mutagenesis

R → A or L: Decreases catalytic activity. Decreases affinity for acetate. Ref.5 Ref.7

Mutagenesis

V → A: Decreases affinity for acetate. Ref.4

Mutagenesis

122

L → A: Decreases affinity for acetate. Ref.4

Mutagenesis

148

D → A, E or N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP. Ref.3

Mutagenesis

179

F → A: Decreases affinity for acetate. Ref.4

Mutagenesis

211

N → A: Slightly reduced enzyme activity. Ref.3

Mutagenesis

232

P → A: Decreases affinity for acetate. Ref.4

Mutagenesis

241

R → K or L: Decreases catalytic activity. Strongly reduced affinity for ATP. Ref.5 Ref.7

Mutagenesis

384

E → A: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Requires strongly increased magnesium levels for enzyme activity. Ref.3

Secondary structure

408

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P38502 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 1A484DF8A7258800
Show »

FASTA

408

44,337

        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

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References

[1]	"Cloning, sequence analysis, and hyperexpression of the genes encoding phosphotransacetylase and acetate kinase from Methanosarcina thermophila." Latimer M.T., Ferry J.G. J. Bacteriol. 175:6822-6829(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: DSM 1825 / TM-1.
[2]	"Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila. Evidence for regulation of synthesis." Aceti D.J., Ferry J.G. J. Biol. Chem. 263:15444-15448(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-17, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
[3]	"Site-directed mutational analysis of active site residues in the acetate kinase from Methanosarcina thermophila." Miles R.D., Iyer P.P., Ferry J.G. J. Biol. Chem. 276:45059-45064(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, MUTAGENESIS OF ASN-7; SER-10; SER-12; LYS-14; ASP-148; ASN-211 AND GLU-384.
[4]	"Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase." Ingram-Smith C., Gorrell A., Lawrence S.H., Iyer P., Smith K., Ferry J.G. J. Bacteriol. 187:2386-2394(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF VAL-93; LEU-122; PHE-179 AND PRO-232.
[5]	"Investigation of the Methanosarcina thermophila acetate kinase mechanism by fluorescence quenching." Gorrell A., Ferry J.G. Biochemistry 46:14170-14176(2007) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-91 AND ARG-241.
[6]	"Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases." Buss K.A., Cooper D.R., Ingram-Smith C., Ferry J.G., Sanders D.A., Hasson M.S. J. Bacteriol. 183:680-686(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ADP, ACTIVE SITE, SUBUNIT.
[7]	"Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila." Gorrell A., Lawrence S.H., Ferry J.G. J. Biol. Chem. 280:10731-10742(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-399 IN COMPLEX WITH ADP; AMP; ALF3 AND ACETATE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, ENZYME REGULATION, COFACTOR, SUBUNIT, MUTAGENESIS OF ARG-91 AND ARG-241.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L23147 Unassigned DNA. Translation: AAA72042.1.

PIR

B49338.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G99	X-ray	2.50	A/B	1-408	[»]
1TUU	X-ray	2.50	A/B	1-399	[»]
1TUY	X-ray	3.00	A/B	1-399	[»]

ProteinModelPortal

P38502.

SMR

P38502. Positions 1-399.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P38502.

UniPathway

UPA00340; UER00458.

Family and domain databases

HAMAP

MF_00020. Acetate_kinase.

InterPro

IPR004372. Ac/Proprionate_kinase.
IPR000890. Aliphatic_acid_kin_short-chain.
IPR023865. Aliphatic_acid_kinase_CS.
[Graphical view]

PANTHER

PTHR21060. PTHR21060. 1 hit.

Pfam

PF00871. Acetate_kinase. 1 hit.
[Graphical view]

PIRSF

PIRSF000722. Acetate_prop_kin. 1 hit.

PRINTS

PR00471. ACETATEKNASE.

TIGRFAMs

TIGR00016. ackA. 1 hit.

PROSITE

PS01075. ACETATE_KINASE_1. 1 hit.
PS01076. ACETATE_KINASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

EvolutionaryTrace

P38502.

Entry information

Entry name

ACKA_METTE

Accession

Primary (citable) accession number: P38502

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents