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P38502 (ACKA_METTE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetate kinase

EC=2.7.2.1
Alternative name(s):
Acetokinase
Gene names
Name:ackA
Synonyms:ack
OrganismMethanosarcina thermophila
Taxonomic identifier2210 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Protein existenceEvidence 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 HAMAP-Rule MF_00020.

Sequence similarities

Belongs to the acetokinase family.

Biophysicochemical properties

Kinetic parameters:

KM=71 µM for ATP Ref.1 Ref.2 Ref.4 Ref.5 Ref.7

KM=98 µM for ADP

KM=1.5 mM for acetate

KM=0.47 mM for acetyl phosphate

Temperature dependence:

Optimum temperature is 65 degrees Celsius. Protected from thermal inactivation by ATP.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processacetyl-CoA biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

organic acid metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 408408Acetate kinase HAMAP-Rule MF_00020
PRO_0000107650

Regions

Nucleotide binding208 – 2125ATP HAMAP-Rule MF_00020
Nucleotide binding283 – 2853ATP HAMAP-Rule MF_00020
Nucleotide binding331 – 3355ATP HAMAP-Rule MF_00020

Sites

Active site1481Proton donor/acceptor Ref.6 Ref.7
Metal binding71Magnesium Probable
Metal binding3841Magnesium Probable
Binding site141ATP
Binding site911Substrate
Site1801Transition state stabilizer
Site2411Transition state stabilizer

Experimental info

Mutagenesis71N → A: Almost abolishes catalytic activity. Requires increased magnesium levels for activity. Strongly decreases affinity for acetate. Ref.3
Mutagenesis71N → D: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Ref.3
Mutagenesis101S → A or T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate. Ref.3
Mutagenesis111S → A: Decreases catalytic activity. Decreases affinity for acetate.
Mutagenesis111S → T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate.
Mutagenesis121S → A: Decreases catalytic activity. Strongly decreases affinity for acetate. Requires increased magnesium levels for enzyme activity. Ref.3
Mutagenesis121S → T: Decreases catalytic activity. Strongly decreases affinity for acetate. Ref.3
Mutagenesis141K → A: Strongly decreases enzyme activity. Ref.3
Mutagenesis141K → R: Reduces enzyme activity. Ref.3
Mutagenesis911R → A or L: Decreases catalytic activity. Decreases affinity for acetate. Ref.5 Ref.7
Mutagenesis931V → A: Decreases affinity for acetate. Ref.4
Mutagenesis1221L → A: Decreases affinity for acetate. Ref.4
Mutagenesis1481D → A, E or N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP. Ref.3
Mutagenesis1791F → A: Decreases affinity for acetate. Ref.4
Mutagenesis2111N → A: Slightly reduced enzyme activity. Ref.3
Mutagenesis2321P → A: Decreases affinity for acetate. Ref.4
Mutagenesis2411R → K or L: Decreases catalytic activity. Strongly reduced affinity for ATP. Ref.5 Ref.7
Mutagenesis3841E → 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 LengthMass (Da)Tools
P38502 [UniParc].

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

FASTA40844,337
        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 

« Hide

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L23147 Unassigned DNA. Translation: AAA72042.1.
PIRB49338.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G99X-ray2.50A/B1-408[»]
1TUUX-ray2.50A/B1-399[»]
1TUYX-ray3.00A/B1-399[»]
ProteinModelPortalP38502.
SMRP38502. Positions 1-399.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB00131. Adenosine monophosphate.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP38502.
UniPathwayUPA00340; UER00458.

Family and domain databases

HAMAPMF_00020. Acetate_kinase.
InterProIPR004372. Ac/Proprionate_kinase.
IPR000890. Aliphatic_acid_kin_short-chain.
IPR023865. Aliphatic_acid_kinase_CS.
[Graphical view]
PANTHERPTHR21060. PTHR21060. 1 hit.
PfamPF00871. Acetate_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF000722. Acetate_prop_kin. 1 hit.
PRINTSPR00471. ACETATEKNASE.
TIGRFAMsTIGR00016. ackA. 1 hit.
PROSITEPS01075. ACETATE_KINASE_1. 1 hit.
PS01076. ACETATE_KINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38502.

Entry information

Entry nameACKA_METTE
AccessionPrimary (citable) accession number: P38502
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: February 19, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways