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P38502

- ACKA_METTE

UniProt

P38502 - ACKA_METTE

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Protein
Acetate kinase
Gene
ackA, ack
Organism
Methanosarcina thermophila
Status
Reviewed - 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.1 Publication

Catalytic activityi

ATP + acetate = ADP + acetyl phosphate.6 Publications

Cofactori

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

Enzyme regulationi

Inhibited by diethylpyrocarbonate, hydroxylamine and phenylglyoxal.2 Publications

Kineticsi

  1. KM=71 µM for ATP5 Publications
  2. KM=98 µM for ADP
  3. KM=1.5 mM for acetate
  4. KM=0.47 mM for acetyl phosphate

Temperature dependencei

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi7 – 71Magnesium Inferred
Binding sitei14 – 141ATP
Binding sitei91 – 911Substrate
Active sitei148 – 1481Proton donor/acceptor2 Publications
Sitei180 – 1801Transition state stabilizer
Sitei241 – 2411Transition state stabilizer
Metal bindingi384 – 3841Magnesium Inferred

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. acetate kinase activity Source: UniProtKB-HAMAP
  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
Complete GO annotation...

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 kinase (EC:2.7.2.1)
Alternative name(s):
Acetokinase
Gene namesi
Name:ackA
Synonyms:ack
OrganismiMethanosarcina thermophila
Taxonomic identifieri2210 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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 kinaseUniRule annotation
PRO_0000107650Add
BLAST

Interactioni

Subunit structurei

Homodimer.5 Publications

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP38502.

Family & Domainsi

Sequence similaritiesi

Belongs to the acetokinase family.

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...

Chemistry

DrugBanki DB00131. Adenosine monophosphate.

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 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.

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: February 19, 2014
This is version 91 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

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