UniProtKB - P0A9M8 (PTA_ECOLI)
Protein
Phosphate acetyltransferase
Gene
pta
Organism
Escherichia coli (strain K12)
Status
Functioni
Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. On minimal medium acetyl-CoA is generated. In rich medium acetyl-CoA is converted to acetate and allowing the cell to dump the excess of acetylation potential in exchange for energy in the form of ATP (PubMed:15687190). The main pathway for acetate production during exponential phase (PubMed:16080684).2 Publications
Catalytic activityi
- EC:2.3.1.8
Activity regulationi
Inhibited by NADH and ATP. Pyruvate and PEP act as activators of the acetyl phosphate forming reaction while inhibiting the formation of acetyl-CoA.1 Publication
Kineticsi
- KM=67.2 µM for acetyl-CoA1 Publication
- KM=44.9 µM for acetyl phosphate1 Publication
- Vmax=177.4 µM/h/mg enzyme for acetyl-CoA-forming reaction1 Publication
- Vmax=23.1 µM/h/mg enzyme for acetyl phosphate-forming reaction1 Publication
: acetyl-CoA biosynthesis Pathwayi
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:
- Acetate kinase (ackA), Acetate kinase (ackA)
- Phosphate acetyltransferase (FAZ83_00825), Phosphate acetyltransferase (pta)
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
- phosphate acetyltransferase activity Source: EcoCyc
- zinc ion binding Source: EcoliWiki
GO - Biological processi
- acetate biosynthetic process Source: EcoCyc
- acetate catabolic process Source: EcoCyc
- acetate metabolic process Source: CACAO
- acetyl-CoA biosynthetic process from acetate Source: EcoCyc
- L-threonine catabolic process to propionate Source: EcoCyc
Keywordsi
Molecular function | Acyltransferase, Transferase |
Enzyme and pathway databases
BioCyci | EcoCyc:PHOSACETYLTRANS-MONOMER MetaCyc:PHOSACETYLTRANS-MONOMER |
BRENDAi | 2.3.1.8, 2026 |
UniPathwayi | UPA00340;UER00459 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:pta Ordered Locus Names:b2297, JW2294 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm Curated
GO - Cellular componenti
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
Severe impairment of growth in anaerobic conditions, as well as in growth on minimal medium. Increased sensitivity to environmental changes. Poor starvation survival and slower growth on glucose, fructose, tryptone broth, or pyruvate, but normal growth on glycerol or succinate.3 Publications
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000179129 | 2 – 714 | Phosphate acetyltransferaseAdd BLAST | 713 |
Proteomic databases
jPOSTi | P0A9M8 |
PaxDbi | P0A9M8 |
PRIDEi | P0A9M8 |
2D gel databases
SWISS-2DPAGEi | P0A9M8 |
Expressioni
Inductioni
Expressed during exponential phase, decreases as cells enter stationary phase at pH 7.0. Expression is inhibited at pH 6.0. Part of the ackA-pta operon.1 Publication
Interactioni
Subunit structurei
Homohexamer.
1 PublicationBinary interactionsi
Hide detailsP0A9M8
With | #Exp. | IntAct |
---|---|---|
chpS [P08365] | 3 | EBI-555015,EBI-556499 |
napD [P0A9I5] | 3 | EBI-555015,EBI-554985 |
yjgH [P39332] | 2 | EBI-555015,EBI-561380 |
Protein-protein interaction databases
BioGRIDi | 4261500, 351 interactors 851119, 1 interactor |
DIPi | DIP-35815N |
IntActi | P0A9M8, 28 interactors |
STRINGi | 511145.b2297 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 391 – 714 | Phosphate acetyltransferaseAdd BLAST | 324 |
Domaini
The N-terminal region seems to be important for proper quaternary structure. The C-terminal region contains the substrate-binding site.1 Publication
Sequence similaritiesi
In the N-terminal section; belongs to the CobB/CobQ family.Curated
In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.Curated
Phylogenomic databases
eggNOGi | COG0280, Bacteria COG0857, Bacteria |
InParanoidi | P0A9M8 |
PhylomeDBi | P0A9M8 |
Family and domain databases
Gene3Di | 3.40.1390.20, 1 hit 3.40.50.10750, 1 hit 3.40.50.10950, 1 hit |
InterProi | View protein in InterPro IPR010766, DRTGG IPR016475, P-Actrans_bac IPR027417, P-loop_NTPase IPR004614, P_AcTrfase IPR042113, P_AcTrfase_dom1 IPR042112, P_AcTrfase_dom2 IPR002505, PTA_PTB IPR028979, Ser_kin/Pase_Hpr-like_N_sf |
Pfami | View protein in Pfam PF07085, DRTGG, 1 hit PF01515, PTA_PTB, 1 hit |
PIRSFi | PIRSF006107, PhpActrans_proteobac, 1 hit |
SUPFAMi | SSF52540, SSF52540, 1 hit SSF75138, SSF75138, 1 hit |
TIGRFAMsi | TIGR00651, pta, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A9M8-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSRIIMLIPT GTSVGLTSVS LGVIRAMERK GVRLSVFKPI AQPRTGGDAP
60 70 80 90 100
DQTTTIVRAN SSTTTAAEPL KMSYVEGLLS SNQKDVLMEE IVANYHANTK
110 120 130 140 150
DAEVVLVEGL VPTRKHQFAQ SLNYEIAKTL NAEIVFVMSQ GTDTPEQLKE
160 170 180 190 200
RIELTRNSFG GAKNTNITGV IVNKLNAPVD EQGRTRPDLS EIFDDSSKAK
210 220 230 240 250
VNNVDPAKLQ ESSPLPVLGA VPWSFDLIAT RAIDMARHLN ATIINEGDIN
260 270 280 290 300
TRRVKSVTFC ARSIPHMLEH FRAGSLLVTS ADRPDVLVAA CLAAMNGVEI
310 320 330 340 350
GALLLTGGYE MDARISKLCE RAFATGLPVF MVNTNTWQTS LSLQSFNLEV
360 370 380 390 400
PVDDHERIEK VQEYVANYIN ADWIESLTAT SERSRRLSPP AFRYQLTELA
410 420 430 440 450
RKAGKRIVLP EGDEPRTVKA AAICAERGIA TCVLLGNPAE INRVAASQGV
460 470 480 490 500
ELGAGIEIVD PEVVRESYVG RLVELRKNKG MTETVAREQL EDNVVLGTLM
510 520 530 540 550
LEQDEVDGLV SGAVHTTANT IRPPLQLIKT APGSSLVSSV FFMLLPEQVY
560 570 580 590 600
VYGDCAINPD PTAEQLAEIA IQSADSAAAF GIEPRVAMLS YSTGTSGAGS
610 620 630 640 650
DVEKVREATR LAQEKRPDLM IDGPLQYDAA VMADVAKSKA PNSPVAGRAT
660 670 680 690 700
VFIFPDLNTG NTTYKAVQRS ADLISIGPML QGMRKPVNDL SRGALVDDIV
710
YTIALTAIQS AQQQ
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 20 – 50 | SLGVI…GGDAP → AWRDPCNGTQRRSSERFQTY RSAAYRWRCA in BAA04663 (PubMed:7918659).CuratedAdd BLAST | 31 | |
Sequence conflicti | 208 – 209 | KL → NV in BAA04502 (PubMed:7883769).Curated | 2 | |
Sequence conflicti | 208 – 209 | KL → NV in BAA04663 (PubMed:7918659).Curated | 2 | |
Sequence conflicti | 263 – 271 | SIPHMLEHF → QHSAHAGAL in BAA04663 (PubMed:7918659).Curated | 9 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D17576 Genomic DNA Translation: BAA04502.1 D21123 Genomic DNA Translation: BAA04663.1 U00096 Genomic DNA Translation: AAC75357.1 AP009048 Genomic DNA Translation: BAA16136.1 |
PIRi | G65001 JX0357 S50130 |
RefSeqi | NP_416800.1, NC_000913.3 WP_000086722.1, NZ_STEB01000008.1 |
Genome annotation databases
EnsemblBacteriai | AAC75357; AAC75357; b2297 BAA16136; BAA16136; BAA16136 |
GeneIDi | 48109661 946778 |
KEGGi | ecj:JW2294 eco:b2297 |
PATRICi | fig|1411691.4.peg.4437 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D17576 Genomic DNA Translation: BAA04502.1 D21123 Genomic DNA Translation: BAA04663.1 U00096 Genomic DNA Translation: AAC75357.1 AP009048 Genomic DNA Translation: BAA16136.1 |
PIRi | G65001 JX0357 S50130 |
RefSeqi | NP_416800.1, NC_000913.3 WP_000086722.1, NZ_STEB01000008.1 |
3D structure databases
SMRi | P0A9M8 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4261500, 351 interactors 851119, 1 interactor |
DIPi | DIP-35815N |
IntActi | P0A9M8, 28 interactors |
STRINGi | 511145.b2297 |
2D gel databases
SWISS-2DPAGEi | P0A9M8 |
Proteomic databases
jPOSTi | P0A9M8 |
PaxDbi | P0A9M8 |
PRIDEi | P0A9M8 |
Genome annotation databases
EnsemblBacteriai | AAC75357; AAC75357; b2297 BAA16136; BAA16136; BAA16136 |
GeneIDi | 48109661 946778 |
KEGGi | ecj:JW2294 eco:b2297 |
PATRICi | fig|1411691.4.peg.4437 |
Organism-specific databases
EchoBASEi | EB4147 |
Phylogenomic databases
eggNOGi | COG0280, Bacteria COG0857, Bacteria |
InParanoidi | P0A9M8 |
PhylomeDBi | P0A9M8 |
Enzyme and pathway databases
UniPathwayi | UPA00340;UER00459 |
BioCyci | EcoCyc:PHOSACETYLTRANS-MONOMER MetaCyc:PHOSACETYLTRANS-MONOMER |
BRENDAi | 2.3.1.8, 2026 |
Miscellaneous databases
PROi | PR:P0A9M8 |
Family and domain databases
Gene3Di | 3.40.1390.20, 1 hit 3.40.50.10750, 1 hit 3.40.50.10950, 1 hit |
InterProi | View protein in InterPro IPR010766, DRTGG IPR016475, P-Actrans_bac IPR027417, P-loop_NTPase IPR004614, P_AcTrfase IPR042113, P_AcTrfase_dom1 IPR042112, P_AcTrfase_dom2 IPR002505, PTA_PTB IPR028979, Ser_kin/Pase_Hpr-like_N_sf |
Pfami | View protein in Pfam PF07085, DRTGG, 1 hit PF01515, PTA_PTB, 1 hit |
PIRSFi | PIRSF006107, PhpActrans_proteobac, 1 hit |
SUPFAMi | SSF52540, SSF52540, 1 hit SSF75138, SSF75138, 1 hit |
TIGRFAMsi | TIGR00651, pta, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PTA_ECOLI | |
Accessioni | P0A9M8Primary (citable) accession number: P0A9M8 Secondary accession number(s): P39184 Q9EUP2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 19, 2005 |
Last sequence update: | January 23, 2007 | |
Last modified: | December 2, 2020 | |
This is version 127 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families