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P38503 (PTAS_METTE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphate acetyltransferase

EC=2.3.1.8
Alternative name(s):
Phosphotransacetylase
Gene names
Name:pta
OrganismMethanosarcina thermophila
Taxonomic identifier2210 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + phosphate = CoA + acetyl phosphate.

Pathway

Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.

Subunit structure

Homodimer. Ref.3

Subcellular location

Cell membrane; Peripheral membrane protein.

Sequence similarities

Belongs to the phosphate acetyltransferase and butyryltransferase family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processacetyl-CoA biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphate acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 333332Phosphate acetyltransferase
PRO_0000179151

Experimental info

Mutagenesis1591C → A: Loss of activity.
Mutagenesis1591C → S: No loss of activity.

Secondary structure

.............................................................. 333
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38503 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: EC87B47A387B8398

FASTA33335,220
        10         20         30         40         50         60 
MVTFLEKISE RAKKLNKTIA LPETEDIRTL QAAAKILERG IADIVLVGNE ADIKALAGDL 

        70         80         90        100        110        120 
DLSKAKIVDP KTYEKKDEYI NAFYELRKHK GITLENAAEI MSDYVYFAVM MAKLGEVDGV 

       130        140        150        160        170        180 
VSGAAHSSSD TLRPAVQIVK TAKGAALASA FFIISVPDCE YGSDGTFLFA DSGMVEMPSV 

       190        200        210        220        230        240 
EDVANIAVIS AKTFELLVQD VPKVAMLSYS TKGSAKSKLT EATIASTKLA QELAPDIAID 

       250        260        270        280        290        300 
GELQVDAAIV PKVAASKAPG SPVAGKANVF IFPDLNCGNI AYKIAQRLAK AEAYGPITQG 

       310        320        330 
LAKPINDLSR GCSDEDIVGA VAITCVQAAA QDK 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L23147 Unassigned DNA. Translation: AAA72041.1.
PIRA49338.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QZTX-ray2.70A/B/C/D1-333[»]
2AF3X-ray2.60C/D1-333[»]
2AF4X-ray2.15C/D1-333[»]
ProteinModelPortalP38503.
SMRP38503. Positions 2-333.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP38503.
UniPathwayUPA00340; UER00459.

Family and domain databases

InterProIPR012147. P_Ac_Bu_trans.
IPR004614. P_AcTrfase.
IPR002505. PTA_PTB.
[Graphical view]
PfamPF01515. PTA_PTB. 1 hit.
[Graphical view]
PIRSFPIRSF000428. P_Ac_trans. 1 hit.
TIGRFAMsTIGR00651. pta. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP38503.

Entry information

Entry namePTAS_METTE
AccessionPrimary (citable) accession number: P38503
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 79 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways