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Protein

Phosphate acetyltransferase

Gene

pta

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.1 Publication

Catalytic activityi

Acetyl-CoA + phosphate = CoA + acetyl phosphate.

Enzyme 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

  1. KM=67.2 µM for acetyl-CoA1 Publication
  2. KM=44.9 µM for acetyl phosphate1 Publication
  1. Vmax=177.4 µM/h/mg enzyme for acetyl-CoA-forming reaction1 Publication
  2. Vmax=23.1 µM/h/mg enzyme for acetyl phosphate-forming reaction1 Publication

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

  • 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 functionAcyltransferase, Transferase

Enzyme and pathway databases

BioCyciEcoCyc:PHOSACETYLTRANS-MONOMER
MetaCyc:PHOSACETYLTRANS-MONOMER
BRENDAi2.3.1.8 2026
UniPathwayiUPA00340; UER00459

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphate acetyltransferase (EC:2.3.1.8)
Alternative name(s):
Phosphotransacetylase
Gene namesi
Name:pta
Ordered Locus Names:b2297, JW2294
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG20173 pta

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & 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.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001791292 – 714Phosphate acetyltransferaseAdd BLAST713

Proteomic databases

EPDiP0A9M8
PaxDbiP0A9M8
PRIDEiP0A9M8

2D gel databases

SWISS-2DPAGEP0A9M8

Interactioni

Subunit structurei

Homohexamer.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi4261500, 351 interactors
DIPiDIP-35815N
IntActiP0A9M8, 28 interactors
STRINGi316385.ECDH10B_2459

Structurei

3D structure databases

ProteinModelPortaliP0A9M8
SMRiP0A9M8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni391 – 714Phosphate acetyltransferaseAdd BLAST324

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

eggNOGiENOG4105C6K Bacteria
COG0280 LUCA
COG0857 LUCA
HOGENOMiHOG000053797
InParanoidiP0A9M8
KOiK13788
OMAiTPLMFEY
PhylomeDBiP0A9M8

Family and domain databases

Gene3Di3.40.1390.20, 1 hit
InterProiView protein in InterPro
IPR010766 DRTGG
IPR016475 P-Actrans_bac
IPR027417 P-loop_NTPase
IPR004614 P_AcTrfase
IPR002505 PTA_PTB
IPR028979 Ser_kin/Pase_Hpr-like_N_sf
PfamiView protein in Pfam
PF07085 DRTGG, 1 hit
PF01515 PTA_PTB, 1 hit
PIRSFiPIRSF006107 PhpActrans_proteobac, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF75138 SSF75138, 1 hit
TIGRFAMsiTIGR00651 pta, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0A9M8-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:714
Mass (Da):77,172
Last modified:January 23, 2007 - v2
Checksum:iB45AF0C93494A04C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti20 – 50SLGVI…GGDAP → AWRDPCNGTQRRSSERFQTY RSAAYRWRCA in BAA04663 (PubMed:7918659).CuratedAdd BLAST31
Sequence conflicti208 – 209KL → NV in BAA04502 (PubMed:7883769).Curated2
Sequence conflicti208 – 209KL → NV in BAA04663 (PubMed:7918659).Curated2
Sequence conflicti263 – 271SIPHMLEHF → QHSAHAGAL in BAA04663 (PubMed:7918659).Curated9

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
PIRiG65001
JX0357
S50130
RefSeqiNP_416800.1, NC_000913.3
WP_000086722.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75357; AAC75357; b2297
BAA16136; BAA16136; BAA16136
GeneIDi946778
KEGGiecj:JW2294
eco:b2297
PATRICifig|1411691.4.peg.4437

Similar proteinsi

Entry informationi

Entry nameiPTA_ECOLI
AccessioniPrimary (citable) accession number: P0A9M8
Secondary accession number(s): P39184
, P78091, P78189, P78190, Q9EUP2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 110 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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