Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0A9M8

- PTA_ECOLI

UniProt

P0A9M8 - PTA_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Phosphate acetyltransferase

Gene

pta

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- 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

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

Pathwayi

GO - Molecular functioni

  1. phosphate acetyltransferase activity Source: EcoCyc
  2. zinc ion binding Source: EcoliWiki

GO - Biological processi

  1. acetate biosynthetic process Source: EcoCyc
  2. acetate catabolic process Source: EcoCyc
  3. acetate metabolic process Source: CACAO
  4. acetyl-CoA biosynthetic process from acetate Source: EcoCyc
  5. L-threonine catabolic process to propionate Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciEcoCyc:PHOSACETYLTRANS-MONOMER.
ECOL316407:JW2294-MONOMER.
MetaCyc:PHOSACETYLTRANS-MONOMER.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG20173. pta.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 714713Phosphate acetyltransferasePRO_0000179129Add
BLAST

Proteomic databases

PaxDbiP0A9M8.
PRIDEiP0A9M8.

2D gel databases

SWISS-2DPAGEP0A9M8.

PTM databases

PhosSiteiP0810425.

Expressioni

Gene expression databases

GenevestigatoriP0A9M8.

Interactioni

Subunit structurei

Homohexamer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
napDP0A9I52EBI-555015,EBI-554985

Protein-protein interaction databases

DIPiDIP-35815N.
IntActiP0A9M8. 27 interactions.
MINTiMINT-1263208.
STRINGi511145.b2297.

Structurei

3D structure databases

ProteinModelPortaliP0A9M8.
SMRiP0A9M8. Positions 403-710.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni391 – 714324Phosphate acetyltransferaseAdd
BLAST

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

eggNOGiCOG0280.
HOGENOMiHOG000053797.
InParanoidiP0A9M8.
KOiK13788.
OMAiKPIAQPH.
OrthoDBiEOG6BKJ5W.
PhylomeDBiP0A9M8.

Family and domain databases

Gene3Di3.40.1390.20. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR010766. DRTGG.
IPR016475. P-Actrans_bac.
IPR027417. P-loop_NTPase.
IPR004614. P_AcTrfase.
IPR002505. PTA_PTB.
IPR028979. Ser_kin/Pase_Hpr_N_like.
[Graphical view]
PfamiPF07085. DRTGG. 1 hit.
PF01515. PTA_PTB. 1 hit.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 5031SLGVI…GGDAP → AWRDPCNGTQRRSSERFQTY RSAAYRWRCA in BAA04663. (PubMed:7918659)CuratedAdd
BLAST
Sequence conflicti208 – 2092KL → NV in BAA04502. (PubMed:7883769)Curated
Sequence conflicti208 – 2092KL → NV in BAA04663. (PubMed:7918659)Curated
Sequence conflicti263 – 2719SIPHMLEHF → QHSAHAGAL in BAA04663. (PubMed:7918659)Curated

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.
YP_490539.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75357; AAC75357; b2297.
BAA16136; BAA16136; BAA16136.
GeneIDi12932506.
946778.
KEGGiecj:Y75_p2263.
eco:b2297.
PATRICi32119965. VBIEscCol129921_2392.

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.
YP_490539.1. NC_007779.1.

3D structure databases

ProteinModelPortali P0A9M8.
SMRi P0A9M8. Positions 403-710.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35815N.
IntActi P0A9M8. 27 interactions.
MINTi MINT-1263208.
STRINGi 511145.b2297.

PTM databases

PhosSitei P0810425.

2D gel databases

SWISS-2DPAGE P0A9M8.

Proteomic databases

PaxDbi P0A9M8.
PRIDEi P0A9M8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75357 ; AAC75357 ; b2297 .
BAA16136 ; BAA16136 ; BAA16136 .
GeneIDi 12932506.
946778.
KEGGi ecj:Y75_p2263.
eco:b2297.
PATRICi 32119965. VBIEscCol129921_2392.

Organism-specific databases

EchoBASEi EB4147.
EcoGenei EG20173. pta.

Phylogenomic databases

eggNOGi COG0280.
HOGENOMi HOG000053797.
InParanoidi P0A9M8.
KOi K13788.
OMAi KPIAQPH.
OrthoDBi EOG6BKJ5W.
PhylomeDBi P0A9M8.

Enzyme and pathway databases

UniPathwayi UPA00340 ; UER00459 .
BioCyci EcoCyc:PHOSACETYLTRANS-MONOMER.
ECOL316407:JW2294-MONOMER.
MetaCyc:PHOSACETYLTRANS-MONOMER.

Miscellaneous databases

PROi P0A9M8.

Gene expression databases

Genevestigatori P0A9M8.

Family and domain databases

Gene3Di 3.40.1390.20. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR010766. DRTGG.
IPR016475. P-Actrans_bac.
IPR027417. P-loop_NTPase.
IPR004614. P_AcTrfase.
IPR002505. PTA_PTB.
IPR028979. Ser_kin/Pase_Hpr_N_like.
[Graphical view ]
Pfami PF07085. DRTGG. 1 hit.
PF01515. PTA_PTB. 1 hit.
[Graphical view ]
PIRSFi PIRSF006107. PhpActrans_proteobac. 1 hit.
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF75138. SSF75138. 1 hit.
TIGRFAMsi TIGR00651. pta. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of the ackA (acetate kinase A)-pta (phosphotransacetylase) operon and complementation analysis of acetate utilization by an ackA-pta deletion mutant of Escherichia coli."
    Kakuda H., Hosono K., Shiroishi K., Ichihara S.
    J. Biochem. 116:916-922(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-12.
    Strain: K12 / KH131.
  2. "Nucleotide sequence of the phosphotransacetylase gene of Escherichia coli strain K12."
    Matsuyama A., Yamamoto-Otake H., Hewitt J., McGillivray R.T.A., Nakano E.
    Biochim. Biophys. Acta 1219:559-562(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-9.
    Strain: K12 / 1100.
  3. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Cloning, expression, and nucleotide sequence of the Escherichia coli K-12 ackA gene."
    Matsuyama A., Yamamoto H., Nakano E.
    J. Bacteriol. 171:577-580(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
    Strain: K12.
  7. "Acetate metabolism in a pta mutant of Escherichia coli W3110: importance of maintaining acetyl coenzyme A flux for growth and survival."
    Chang D.E., Shin S., Rhee J.S., Pan J.G.
    J. Bacteriol. 181:6656-6663(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "A defect in the acetyl coenzyme A<-->acetate pathway poisons recombinational repair-deficient mutants of Escherichia coli."
    Shi I.Y., Stansbury J., Kuzminov A.
    J. Bacteriol. 187:1266-1275(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "An insight into the role of phosphotransacetylase (pta) and the acetate/acetyl-CoA node in Escherichia coli."
    Castano-Cerezo S., Pastor J.M., Renilla S., Bernal V., Iborra J.L., Canovas M.
    Microb. Cell Fact. 8:54-54(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. "Functional dissection of Escherichia coli phosphotransacetylase structural domains and analysis of key compounds involved in activity regulation."
    Campos-Bermudez V.A., Bologna F.P., Andreo C.S., Drincovich M.F.
    FEBS J. 277:1957-1966(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN.

Entry informationi

Entry nameiPTA_ECOLI
AccessioniPrimary (citable) accession number: P0A9M8
Secondary accession number(s): P39184
, P78091, P78189, P78190, Q9EUP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3