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P38502

- ACKA_METTE

UniProt

P38502 - ACKA_METTE

Protein

Acetate kinase

Gene

ackA

Organism
Methanosarcina thermophila
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    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.1 PublicationUniRule annotation

    Catalytic activityi

    ATP + acetate = ADP + acetyl phosphate.6 PublicationsUniRule annotation

    Cofactori

    Mg2+. Can also accept Mn2+. The Mg2+ is bound between two conserved protein residues and the ATP phosphate groups.2 PublicationsUniRule annotation

    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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi7 – 71MagnesiumCurated
    Binding sitei14 – 141ATP
    Binding sitei91 – 911Substrate
    Active sitei148 – 1481Proton donor/acceptor2 PublicationsUniRule annotation
    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

    1. acetate kinase activity Source: UniProtKB-HAMAP
    2. ATP binding Source: UniProtKB-KW
    3. magnesium ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. acetyl-CoA biosynthetic process Source: UniProtKB-UniPathway
    2. organic acid metabolic process Source: InterPro

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    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

    1. cytoplasm Source: UniProtKB-SubCell

    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.5 PublicationsUniRule annotation

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MKVLVINAGS SSLKYQLIDM TNESALAVGL CERIGIDNSI ITQKKFDGKK    50
    LEKLTDLPTH KDALEEVVKA LTDDEFGVIK DMGEINAVGH RVVHGGEKFT 100
    TSALYDEGVE KAIKDCFELA PLHNPPNMMG ISACAEIMPG TPMVIVFDTA 150
    FHQTMPPYAY MYALPYDLYE KHGVRKYGFH GTSHKYVAER AALMLGKPAE 200
    ETKIITCHLG NGSSITAVEG GKSVETSMGF TPLEGLAMGT RCGSIDPAIV 250
    PFLMEKEGLT TREIDTLMNK KSGVLGVSGL SNDFRDLDEA ASKGNRKAEL 300
    ALEIFAYKVK KFIGEYSAVL NGADAVVFTA GIGENSASIR KRILTGLDGI 350
    GIKIDDEKNK IRGQEIDIST PDAKVRVFVI PTNEELAIAR ETKEIVETEV 400
    KLRSSIPV 408
    Length:408
    Mass (Da):44,337
    Last modified:October 1, 1994 - v1
    Checksum:i1A484DF8A7258800
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L23147 Unassigned DNA. Translation: AAA72042.1.
    PIRiB49338.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L23147 Unassigned DNA. Translation: AAA72042.1 .
    PIRi B49338.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P38502.
    SMRi P38502. Positions 1-399.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00340 ; UER00458 .
    SABIO-RK P38502.

    Miscellaneous databases

    EvolutionaryTracei P38502.

    Family and domain databases

    HAMAPi MF_00020. Acetate_kinase.
    InterProi IPR004372. Ac/Proprionate_kinase.
    IPR000890. Aliphatic_acid_kin_short-chain.
    IPR023865. Aliphatic_acid_kinase_CS.
    [Graphical view ]
    PANTHERi PTHR21060. PTHR21060. 1 hit.
    Pfami PF00871. Acetate_kinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000722. Acetate_prop_kin. 1 hit.
    PRINTSi PR00471. ACETATEKNASE.
    TIGRFAMsi TIGR00016. ackA. 1 hit.
    PROSITEi PS01075. ACETATE_KINASE_1. 1 hit.
    PS01076. ACETATE_KINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 92 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