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P38503

- PTAS_METTE

UniProt

P38503 - PTAS_METTE

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Protein

Phosphate acetyltransferase

Gene

pta

Organism
Methanosarcina thermophila
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
Complete GO annotation...

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 – 1513Combined sources
Beta strandi18 – 214Combined sources
Helixi27 – 3913Combined sources
Beta strandi43 – 486Combined sources
Helixi50 – 578Combined sources
Beta strandi65 – 684Combined sources
Turni70 – 723Combined sources
Helixi76 – 8712Combined sources
Helixi88 – 903Combined sources
Helixi94 – 1007Combined sources
Helixi104 – 11310Combined sources
Beta strandi118 – 1225Combined sources
Beta strandi124 – 1263Combined sources
Helixi129 – 13810Combined sources
Beta strandi141 – 1444Combined sources
Beta strandi149 – 1557Combined sources
Beta strandi166 – 1705Combined sources
Beta strandi172 – 1743Combined sources
Helixi180 – 19819Combined sources
Beta strandi203 – 2075Combined sources
Beta strandi211 – 2155Combined sources
Helixi218 – 23316Combined sources
Beta strandi237 – 2437Combined sources
Helixi245 – 2495Combined sources
Helixi251 – 2577Combined sources
Turni264 – 2663Combined sources
Beta strandi269 – 2713Combined sources
Helixi275 – 28713Combined sources
Beta strandi292 – 30312Combined sources
Beta strandi305 – 3073Combined sources
Helixi314 – 33219Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MVTFLEKISE RAKKLNKTIA LPETEDIRTL QAAAKILERG IADIVLVGNE
60 70 80 90 100
ADIKALAGDL DLSKAKIVDP KTYEKKDEYI NAFYELRKHK GITLENAAEI
110 120 130 140 150
MSDYVYFAVM MAKLGEVDGV VSGAAHSSSD TLRPAVQIVK TAKGAALASA
160 170 180 190 200
FFIISVPDCE YGSDGTFLFA DSGMVEMPSV EDVANIAVIS AKTFELLVQD
210 220 230 240 250
VPKVAMLSYS TKGSAKSKLT EATIASTKLA QELAPDIAID GELQVDAAIV
260 270 280 290 300
PKVAASKAPG SPVAGKANVF IFPDLNCGNI AYKIAQRLAK AEAYGPITQG
310 320 330
LAKPINDLSR GCSDEDIVGA VAITCVQAAA QDK
Length:333
Mass (Da):35,220
Last modified:January 23, 2007 - v3
Checksum:iEC87B47A387B8398
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23147 Unassigned DNA. Translation: AAA72041.1.
PIRiA49338.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23147 Unassigned DNA. Translation: AAA72041.1 .
PIRi A49338.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 82 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