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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: Mg2+. Can also accept Mn2+. 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

    Pathwayi: acetyl-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)DescriptionActionsGraphical viewLength
    Metal bindingi7MagnesiumCurated1
    Binding sitei14ATP1
    Binding sitei91Substrate1
    Active sitei148Proton donor/acceptorUniRule annotation2 Publications1
    Sitei180Transition state stabilizer1
    Sitei241Transition state stabilizer1
    Metal bindingi384MagnesiumCurated1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi208 – 212ATP5
    Nucleotide bindingi283 – 285ATP3
    Nucleotide bindingi331 – 335ATP5

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi7N → A: Almost abolishes catalytic activity. Requires increased magnesium levels for activity. Strongly decreases affinity for acetate. 1 Publication1
    Mutagenesisi7N → D: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. 1 Publication1
    Mutagenesisi10S → A or T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate. 1 Publication1
    Mutagenesisi11S → A: Decreases catalytic activity. Decreases affinity for acetate. 1
    Mutagenesisi11S → T: Strongly decreases catalytic activity. Strongly decreases affinity for acetate. 1
    Mutagenesisi12S → A: Decreases catalytic activity. Strongly decreases affinity for acetate. Requires increased magnesium levels for enzyme activity. 1 Publication1
    Mutagenesisi12S → T: Decreases catalytic activity. Strongly decreases affinity for acetate. 1 Publication1
    Mutagenesisi14K → A: Strongly decreases enzyme activity. 1 Publication1
    Mutagenesisi14K → R: Reduces enzyme activity. 1 Publication1
    Mutagenesisi91R → A or L: Decreases catalytic activity. Decreases affinity for acetate. 2 Publications1
    Mutagenesisi93V → A: Decreases affinity for acetate. 1 Publication1
    Mutagenesisi122L → A: Decreases affinity for acetate. 1 Publication1
    Mutagenesisi148D → A, E or N: Abolishes catalytic activity. Decreases affinity for acetate, but not for ATP. 1 Publication1
    Mutagenesisi179F → A: Decreases affinity for acetate. 1 Publication1
    Mutagenesisi211N → A: Slightly reduced enzyme activity. 1 Publication1
    Mutagenesisi232P → A: Decreases affinity for acetate. 1 Publication1
    Mutagenesisi241R → K or L: Decreases catalytic activity. Strongly reduced affinity for ATP. 2 Publications1
    Mutagenesisi384E → A: Almost abolishes catalytic activity. Strongly decreases affinity for acetate. Requires strongly increased magnesium levels for enzyme activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001076501 – 408Acetate kinaseAdd BLAST408

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation5 Publications

    Structurei

    Secondary structure

    1408
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 8Combined sources7
    Beta strandi13 – 19Combined sources7
    Turni20 – 23Combined sources4
    Beta strandi24 – 33Combined sources10
    Beta strandi36 – 38Combined sources3
    Beta strandi40 – 45Combined sources6
    Beta strandi50 – 54Combined sources5
    Helixi60 – 71Combined sources12
    Turni74 – 76Combined sources3
    Helixi82 – 84Combined sources3
    Beta strandi87 – 93Combined sources7
    Turni96 – 98Combined sources3
    Helixi107 – 115Combined sources9
    Helixi117 – 119Combined sources3
    Turni121 – 123Combined sources3
    Helixi124 – 137Combined sources14
    Beta strandi143 – 147Combined sources5
    Helixi150 – 154Combined sources5
    Helixi157 – 160Combined sources4
    Helixi166 – 172Combined sources7
    Helixi181 – 195Combined sources15
    Helixi199 – 201Combined sources3
    Beta strandi203 – 219Combined sources17
    Beta strandi222 – 227Combined sources6
    Beta strandi234 – 236Combined sources3
    Helixi249 – 257Combined sources9
    Helixi261 – 270Combined sources10
    Helixi273 – 278Combined sources6
    Helixi284 – 292Combined sources9
    Helixi296 – 319Combined sources24
    Beta strandi324 – 329Combined sources6
    Helixi330 – 335Combined sources6
    Helixi337 – 344Combined sources8
    Helixi348 – 350Combined sources3
    Helixi358 – 360Combined sources3
    Beta strandi374 – 379Combined sources6
    Helixi384 – 397Combined sources14

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP38502.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acetokinase family.UniRule annotation

    Phylogenomic databases

    KOiK00925.

    Family and domain databases

    HAMAPiMF_00020. Acetate_kinase. 1 hit.
    InterProiIPR004372. Ac/propionate_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.

    Genome annotation databases

    KEGGiag:AAA72042.

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1G99X-ray2.50A/B1-408[»]
    1TUUX-ray2.50A/B1-399[»]
    1TUYX-ray3.00A/B1-399[»]
    ProteinModelPortaliP38502.
    SMRiP38502.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAA72042.

    Phylogenomic databases

    KOiK00925.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiP38502.

    Family and domain databases

    HAMAPiMF_00020. Acetate_kinase. 1 hit.
    InterProiIPR004372. Ac/propionate_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...

    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: November 2, 2016
    This is version 104 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

    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 one 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.