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Protein

Acetate kinase

Gene

ackA

Organism
Methanosarcina thermophila
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication

Catalytic activityi

ATP + acetate = ADP + acetyl phosphate.UniRule annotation6 Publications

Cofactori

Mg2+UniRule annotation2 Publications, Mn2+UniRule annotation2 PublicationsNote: Mg(2+). Can also accept Mn(2+). The Mg2+ is bound between two conserved protein residues and the ATP phosphate groups.UniRule annotation2 Publications

Enzyme regulationi

Inhibited by diethylpyrocarbonate, hydroxylamine and phenylglyoxal.2 Publications

Kineticsi

  1. KM=71 µM for ATP5 Publications
  2. KM=98 µM for ADP5 Publications
  3. KM=1.5 mM for acetate5 Publications
  4. KM=0.47 mM for acetyl phosphate5 Publications

    Temperature dependencei

    Optimum temperature is 65 degrees Celsius. Protected from thermal inactivation by ATP.5 Publications

    Pathway:iacetyl-CoA biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes acetyl-CoA from acetate.UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Acetate kinase (ackA)
    2. Phosphate acetyltransferase (pta)
    This subpathway is part of the pathway acetyl-CoA biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetyl-CoA from acetate, the pathway acetyl-CoA biosynthesis and in Metabolic intermediate biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi7 – 71MagnesiumCurated
    Binding sitei14 – 141ATP
    Binding sitei91 – 911Substrate
    Active sitei148 – 1481Proton donor/acceptorUniRule annotation2 Publications
    Sitei180 – 1801Transition state stabilizer
    Sitei241 – 2411Transition state stabilizer
    Metal bindingi384 – 3841MagnesiumCurated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi208 – 2125ATP
    Nucleotide bindingi283 – 2853ATP
    Nucleotide bindingi331 – 3355ATP

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.2.1. 3281.
    SABIO-RKP38502.
    UniPathwayiUPA00340; UER00458.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetate kinaseUniRule annotation (EC:2.7.2.1UniRule annotation)
    Alternative name(s):
    AcetokinaseUniRule annotation
    Gene namesi
    Name:ackAUniRule annotation
    Synonyms:ack
    OrganismiMethanosarcina thermophila
    Taxonomic identifieri2210 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71N → A: Almost abolishes catalytic activity. Requires increased magnesium levels for activity. Strongly decreases affinity for acetate. 1 Publication
    Mutagenesisi7 – 71N → D: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. 1 Publication
    Mutagenesisi10 – 101S → A or T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate. 1 Publication
    Mutagenesisi11 – 111S → A: Decreases catalytic activity. Decreases affinity for acetate.
    Mutagenesisi11 – 111S → T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate.
    Mutagenesisi12 – 121S → A: Decreases catalytic activity. Strongly decreases affinity for acetate. Requires increased magnesium levels for enzyme activity. 1 Publication
    Mutagenesisi12 – 121S → T: Decreases catalytic activity. Strongly decreases affinity for acetate. 1 Publication
    Mutagenesisi14 – 141K → A: Strongly decreases enzyme activity. 1 Publication
    Mutagenesisi14 – 141K → R: Reduces enzyme activity. 1 Publication
    Mutagenesisi91 – 911R → A or L: Decreases catalytic activity. Decreases affinity for acetate. 2 Publications
    Mutagenesisi93 – 931V → A: Decreases affinity for acetate. 1 Publication
    Mutagenesisi122 – 1221L → A: Decreases affinity for acetate. 1 Publication
    Mutagenesisi148 – 1481D → A, E or N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP. 1 Publication
    Mutagenesisi179 – 1791F → A: Decreases affinity for acetate. 1 Publication
    Mutagenesisi211 – 2111N → A: Slightly reduced enzyme activity. 1 Publication
    Mutagenesisi232 – 2321P → A: Decreases affinity for acetate. 1 Publication
    Mutagenesisi241 – 2411R → K or L: Decreases catalytic activity. Strongly reduced affinity for ATP. 2 Publications
    Mutagenesisi384 – 3841E → A: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Requires strongly increased magnesium levels for enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 408408Acetate kinasePRO_0000107650Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation5 Publications

    Structurei

    Secondary structure

    1
    408
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 87Combined sources
    Beta strandi13 – 197Combined sources
    Turni20 – 234Combined sources
    Beta strandi24 – 3310Combined sources
    Beta strandi36 – 383Combined sources
    Beta strandi40 – 456Combined sources
    Beta strandi50 – 545Combined sources
    Helixi60 – 7112Combined sources
    Turni74 – 763Combined sources
    Helixi82 – 843Combined sources
    Beta strandi87 – 937Combined sources
    Turni96 – 983Combined sources
    Helixi107 – 1159Combined sources
    Helixi117 – 1193Combined sources
    Turni121 – 1233Combined sources
    Helixi124 – 13714Combined sources
    Beta strandi143 – 1475Combined sources
    Helixi150 – 1545Combined sources
    Helixi157 – 1604Combined sources
    Helixi166 – 1727Combined sources
    Helixi181 – 19515Combined sources
    Helixi199 – 2013Combined sources
    Beta strandi203 – 21917Combined sources
    Beta strandi222 – 2276Combined sources
    Beta strandi234 – 2363Combined sources
    Helixi249 – 2579Combined sources
    Helixi261 – 27010Combined sources
    Helixi273 – 2786Combined sources
    Helixi284 – 2929Combined sources
    Helixi296 – 31924Combined sources
    Beta strandi324 – 3296Combined sources
    Helixi330 – 3356Combined sources
    Helixi337 – 3448Combined sources
    Helixi348 – 3503Combined sources
    Helixi358 – 3603Combined sources
    Beta strandi374 – 3796Combined sources
    Helixi384 – 39714Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G99X-ray2.50A/B1-408[»]
    1TUUX-ray2.50A/B1-399[»]
    1TUYX-ray3.00A/B1-399[»]
    ProteinModelPortaliP38502.
    SMRiP38502. Positions 1-399.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38502.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acetokinase family.UniRule annotation

    Family and domain databases

    HAMAPiMF_00020. Acetate_kinase.
    InterProiIPR004372. Ac/Proprionate_kinase.
    IPR000890. Aliphatic_acid_kin_short-chain.
    IPR023865. Aliphatic_acid_kinase_CS.
    [Graphical view]
    PANTHERiPTHR21060. PTHR21060. 1 hit.
    PfamiPF00871. Acetate_kinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000722. Acetate_prop_kin. 1 hit.
    PRINTSiPR00471. ACETATEKNASE.
    TIGRFAMsiTIGR00016. ackA. 1 hit.
    PROSITEiPS01075. ACETATE_KINASE_1. 1 hit.
    PS01076. ACETATE_KINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38502-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKVLVINAGS SSLKYQLIDM TNESALAVGL CERIGIDNSI ITQKKFDGKK
    60 70 80 90 100
    LEKLTDLPTH KDALEEVVKA LTDDEFGVIK DMGEINAVGH RVVHGGEKFT
    110 120 130 140 150
    TSALYDEGVE KAIKDCFELA PLHNPPNMMG ISACAEIMPG TPMVIVFDTA
    160 170 180 190 200
    FHQTMPPYAY MYALPYDLYE KHGVRKYGFH GTSHKYVAER AALMLGKPAE
    210 220 230 240 250
    ETKIITCHLG NGSSITAVEG GKSVETSMGF TPLEGLAMGT RCGSIDPAIV
    260 270 280 290 300
    PFLMEKEGLT TREIDTLMNK KSGVLGVSGL SNDFRDLDEA ASKGNRKAEL
    310 320 330 340 350
    ALEIFAYKVK KFIGEYSAVL NGADAVVFTA GIGENSASIR KRILTGLDGI
    360 370 380 390 400
    GIKIDDEKNK IRGQEIDIST PDAKVRVFVI PTNEELAIAR ETKEIVETEV

    KLRSSIPV
    Length:408
    Mass (Da):44,337
    Last modified:October 1, 1994 - v1
    Checksum:i1A484DF8A7258800
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L23147 Unassigned DNA. Translation: AAA72042.1.
    PIRiB49338.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L23147 Unassigned DNA. Translation: AAA72042.1.
    PIRiB49338.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G99X-ray2.50A/B1-408[»]
    1TUUX-ray2.50A/B1-399[»]
    1TUYX-ray3.00A/B1-399[»]
    ProteinModelPortaliP38502.
    SMRiP38502. Positions 1-399.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00340; UER00458.
    BRENDAi2.7.2.1. 3281.
    SABIO-RKP38502.

    Miscellaneous databases

    EvolutionaryTraceiP38502.

    Family and domain databases

    HAMAPiMF_00020. Acetate_kinase.
    InterProiIPR004372. Ac/Proprionate_kinase.
    IPR000890. Aliphatic_acid_kin_short-chain.
    IPR023865. Aliphatic_acid_kinase_CS.
    [Graphical view]
    PANTHERiPTHR21060. PTHR21060. 1 hit.
    PfamiPF00871. Acetate_kinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000722. Acetate_prop_kin. 1 hit.
    PRINTSiPR00471. ACETATEKNASE.
    TIGRFAMsiTIGR00016. ackA. 1 hit.
    PROSITEiPS01075. ACETATE_KINASE_1. 1 hit.
    PS01076. ACETATE_KINASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    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 THE ATP ANALOG 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 THE ATP ANALOGS ADP; AMP; ALF3 AND THE SUBSTRATE ACETATE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, ENZYME REGULATION, COFACTOR, SUBUNIT, MUTAGENESIS OF ARG-91 AND ARG-241.

    Entry informationi

    Entry nameiACKA_METTE
    AccessioniPrimary (citable) accession number: P38502
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: April 1, 2015
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.