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Protein

Phosphate acetyltransferase

Gene

pta

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

Functioni

Catalytic activityi

Acetyl-CoA + phosphate = CoA + acetyl phosphate.

Pathwayi: acetyl-CoA biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes acetyl-CoA from acetate.
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.8. 3281.
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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi159C → A: Loss of activity. 1 Publication1
Mutagenesisi159C → S: No loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001791512 – 333Phosphate acetyltransferaseAdd BLAST332

Proteomic databases

PRIDEiP38503.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 15Combined sources13
Beta strandi18 – 21Combined sources4
Helixi27 – 39Combined sources13
Beta strandi43 – 48Combined sources6
Helixi50 – 57Combined sources8
Beta strandi65 – 68Combined sources4
Turni70 – 72Combined sources3
Helixi76 – 87Combined sources12
Helixi88 – 90Combined sources3
Helixi94 – 100Combined sources7
Helixi104 – 113Combined sources10
Beta strandi118 – 122Combined sources5
Beta strandi124 – 126Combined sources3
Helixi129 – 138Combined sources10
Beta strandi141 – 144Combined sources4
Beta strandi149 – 155Combined sources7
Beta strandi166 – 170Combined sources5
Beta strandi172 – 174Combined sources3
Helixi180 – 198Combined sources19
Beta strandi203 – 207Combined sources5
Beta strandi211 – 215Combined sources5
Helixi218 – 233Combined sources16
Beta strandi237 – 243Combined sources7
Helixi245 – 249Combined sources5
Helixi251 – 257Combined sources7
Turni264 – 266Combined sources3
Beta strandi269 – 271Combined sources3
Helixi275 – 287Combined sources13
Beta strandi292 – 303Combined sources12
Beta strandi305 – 307Combined sources3
Helixi314 – 332Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QZTX-ray2.70A/B/C/D1-333[»]
2AF3X-ray2.60C/D1-333[»]
2AF4X-ray2.15C/D1-333[»]
ProteinModelPortaliP38503.
SMRiP38503.
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.
PIRiA49338.

3D structure databases

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

Proteomic databases

PRIDEiP38503.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00340; UER00459.
BRENDAi2.3.1.8. 3281.
SABIO-RKP38503.

Miscellaneous databases

EvolutionaryTraceiP38503.

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.
ProtoNetiSearch...

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 2, 2016
This is version 89 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

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.