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P38503

- PTAS_METTE

UniProt

P38503 - PTAS_METTE

Protein

Phosphate acetyltransferase

Gene

pta

Organism
Methanosarcina thermophila
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Acetyl-CoA + phosphate = CoA + acetyl phosphate.

    Pathwayi

    GO - Molecular functioni

    1. phosphate acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. acetyl-CoA biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    SABIO-RKP38503.
    UniPathwayiUPA00340; UER00459.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphate acetyltransferase (EC:2.3.1.8)
    Alternative name(s):
    Phosphotransacetylase
    Gene namesi
    Name:pta
    OrganismiMethanosarcina thermophila
    Taxonomic identifieri2210 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

    Subcellular locationi

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi159 – 1591C → A: Loss of activity. 1 Publication
    Mutagenesisi159 – 1591C → S: No loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 333332Phosphate acetyltransferasePRO_0000179151Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    333
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1513
    Beta strandi18 – 214
    Helixi27 – 3913
    Beta strandi43 – 486
    Helixi50 – 578
    Beta strandi65 – 684
    Turni70 – 723
    Helixi76 – 8712
    Helixi88 – 903
    Helixi94 – 1007
    Helixi104 – 11310
    Beta strandi118 – 1225
    Beta strandi124 – 1263
    Helixi129 – 13810
    Beta strandi141 – 1444
    Beta strandi149 – 1557
    Beta strandi166 – 1705
    Beta strandi172 – 1743
    Helixi180 – 19819
    Beta strandi203 – 2075
    Beta strandi211 – 2155
    Helixi218 – 23316
    Beta strandi237 – 2437
    Helixi245 – 2495
    Helixi251 – 2577
    Turni264 – 2663
    Beta strandi269 – 2713
    Helixi275 – 28713
    Beta strandi292 – 30312
    Beta strandi305 – 3073
    Helixi314 – 33219

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QZTX-ray2.70A/B/C/D1-333[»]
    2AF3X-ray2.60C/D1-333[»]
    2AF4X-ray2.15C/D1-333[»]
    ProteinModelPortaliP38503.
    SMRiP38503. Positions 2-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38503.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR012147. P_Ac_Bu_trans.
    IPR004614. P_AcTrfase.
    IPR002505. PTA_PTB.
    [Graphical view]
    PfamiPF01515. PTA_PTB. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000428. P_Ac_trans. 1 hit.
    TIGRFAMsiTIGR00651. pta. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P38503-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVTFLEKISE RAKKLNKTIA LPETEDIRTL QAAAKILERG IADIVLVGNE    50
    ADIKALAGDL DLSKAKIVDP KTYEKKDEYI NAFYELRKHK GITLENAAEI 100
    MSDYVYFAVM MAKLGEVDGV VSGAAHSSSD TLRPAVQIVK TAKGAALASA 150
    FFIISVPDCE YGSDGTFLFA DSGMVEMPSV EDVANIAVIS AKTFELLVQD 200
    VPKVAMLSYS TKGSAKSKLT EATIASTKLA QELAPDIAID GELQVDAAIV 250
    PKVAASKAPG SPVAGKANVF IFPDLNCGNI AYKIAQRLAK AEAYGPITQG 300
    LAKPINDLSR GCSDEDIVGA VAITCVQAAA QDK 333
    Length:333
    Mass (Da):35,220
    Last modified:January 23, 2007 - v3
    Checksum:iEC87B47A387B8398
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L23147 Unassigned DNA. Translation: AAA72041.1.
    PIRiA49338.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L23147 Unassigned DNA. Translation: AAA72041.1 .
    PIRi A49338.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QZT X-ray 2.70 A/B/C/D 1-333 [» ]
    2AF3 X-ray 2.60 C/D 1-333 [» ]
    2AF4 X-ray 2.15 C/D 1-333 [» ]
    ProteinModelPortali P38503.
    SMRi P38503. Positions 2-333.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00340 ; UER00459 .
    SABIO-RK P38503.

    Miscellaneous databases

    EvolutionaryTracei P38503.

    Family and domain databases

    InterProi IPR012147. P_Ac_Bu_trans.
    IPR004614. P_AcTrfase.
    IPR002505. PTA_PTB.
    [Graphical view ]
    Pfami PF01515. PTA_PTB. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000428. P_Ac_trans. 1 hit.
    TIGRFAMsi TIGR00651. pta. 1 hit.
    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], PROTEIN SEQUENCE OF 2-21.
      Strain: DSM 1825 / TM-1.
    2. "Identification of cysteine and arginine residues essential for the phosphotransacetylase from Methanosarcina thermophila."
      Rasche M.E., Smith K.S., Ferry J.G.
      J. Bacteriol. 179:7712-7717(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    3. "Crystal structure of phosphotransacetylase from the methanogenic archaeon Methanosarcina thermophila."
      Iyer P.P., Lawrence S.H., Luther K.B., Rajashankar K.R., Yennawar H.P., Ferry J.G., Schindelin H.
      Structure 12:559-567(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiPTAS_METTE
    AccessioniPrimary (citable) accession number: P38503
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 80 of the entry and version 3 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