P0A9M8 (PTA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphate acetyltransferase
EC=2.3.1.8

Alternative name(s):
Phosphotransacetylase

Gene names

Name:	pta
Ordered Locus Names:	b2297, JW2294

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	714 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8
Catalytic activity	Acetyl-CoA + phosphate = CoA + acetyl phosphate.
Enzyme regulation	Inhibited by NADH and ATP. Pyruvate and PEP act as activators of the acetyl phosphate forming reaction while inhibiting the formation of acetyl-CoA. Ref.10
Pathway	Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subunit structure	Homohexamer. Ref.10
Subcellular location	Cytoplasm Potential.
Domain	The N-terminal region seems to be important for proper quaternary structure. The C-terminal region contains the substrate-binding site. Ref.10
Disruption phenotype	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. Ref.7 Ref.9
Sequence similarities	In the N-terminal section; belongs to the CobB/CobQ family. In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family.
Biophysicochemical properties	Kinetic parameters: KM=67.2 µM for acetyl-CoA Ref.10 KM=44.9 µM for acetyl phosphate Vmax=177.4 µM/h/mg enzyme for acetyl-CoA-forming reaction Vmax=23.1 µM/h/mg enzyme for acetyl phosphate-forming reaction

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	L-threonine catabolic process to propionate Inferred from mutant phenotype. Source: EcoCyc acetate biosynthetic process Inferred from mutant phenotype. Source: EcoCyc acetate catabolic process Inferred from mutant phenotype. Source: EcoCyc acetyl-CoA biosynthetic process from acetate Inferred from mutant phenotype. Source: EcoCyc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	phosphate acetyltransferase activity Inferred from direct assay Ref.10. Source: EcoCyc protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from direct assay. Source: EcoliWiki
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
napD	P0A9I5	2	EBI-555015,EBI-554985

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1 Ref.2
	Chain	2 – 714	713	Phosphate acetyltransferase		PRO_0000179129
Regions
	Region	391 – 714	324	Phosphate acetyltransferase
Experimental info
	Sequence conflict	20 – 50	31	SLGVI…GGDAP → AWRDPCNGTQRRSSERFQTY RSAAYRWRCA in BAA04663. Ref.2
	Sequence conflict	208 – 209	2	KL → NV in BAA04502. Ref.1
	Sequence conflict	208 – 209	2	KL → NV in BAA04663. Ref.2
	Sequence conflict	263 – 271	9	SIPHMLEHF → QHSAHAGAL in BAA04663. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P0A9M8 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: B45AF0C93494A04C	FASTA	714	77,172
	10 20 30 40 50 60 MSRIIMLIPT GTSVGLTSVS LGVIRAMERK GVRLSVFKPI AQPRTGGDAP DQTTTIVRAN 70 80 90 100 110 120 SSTTTAAEPL KMSYVEGLLS SNQKDVLMEE IVANYHANTK DAEVVLVEGL VPTRKHQFAQ 130 140 150 160 170 180 SLNYEIAKTL NAEIVFVMSQ GTDTPEQLKE RIELTRNSFG GAKNTNITGV IVNKLNAPVD 190 200 210 220 230 240 EQGRTRPDLS EIFDDSSKAK VNNVDPAKLQ ESSPLPVLGA VPWSFDLIAT RAIDMARHLN 250 260 270 280 290 300 ATIINEGDIN TRRVKSVTFC ARSIPHMLEH FRAGSLLVTS ADRPDVLVAA CLAAMNGVEI 310 320 330 340 350 360 GALLLTGGYE MDARISKLCE RAFATGLPVF MVNTNTWQTS LSLQSFNLEV PVDDHERIEK 370 380 390 400 410 420 VQEYVANYIN ADWIESLTAT SERSRRLSPP AFRYQLTELA RKAGKRIVLP EGDEPRTVKA 430 440 450 460 470 480 AAICAERGIA TCVLLGNPAE INRVAASQGV ELGAGIEIVD PEVVRESYVG RLVELRKNKG 490 500 510 520 530 540 MTETVAREQL EDNVVLGTLM LEQDEVDGLV SGAVHTTANT IRPPLQLIKT APGSSLVSSV 550 560 570 580 590 600 FFMLLPEQVY VYGDCAINPD PTAEQLAEIA IQSADSAAAF GIEPRVAMLS YSTGTSGAGS 610 620 630 640 650 660 DVEKVREATR LAQEKRPDLM IDGPLQYDAA VMADVAKSKA PNSPVAGRAT VFIFPDLNTG 670 680 690 700 710 NTTYKAVQRS ADLISIGPML QGMRKPVNDL SRGALVDDIV YTIALTAIQS AQQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7883769] [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: 7918659] [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: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 2536666] [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: 10542166] [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: 15687190] [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: 19852855] [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: 20236319] [Abstract] Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D17576 Genomic DNA. Translation: BAA04502.1. D21123 Genomic DNA. Translation: BAA04663.1. U00096 Genomic DNA. Translation: AAC75357.1. AP009048 Genomic DNA. Translation: BAA16136.1.
PIR	G65001. JX0357. S50130.
RefSeq	NP_416800.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0A9M8.
SMR	P0A9M8. Positions 3-37, 230-353, 390-714.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-35815N.
IntAct	P0A9M8. 26 interactions.
MINT	MINT-1263208.
PTM databases
PhosSite	P0A9M8.
2D gel databases
SWISS-2DPAGE	P0A9M8.
Proteomic databases
PRIDE	P0A9M8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000004864; EBESCP00000004864; EBESCG00000003969. EBESCT00000018341; EBESCP00000017632; EBESCG00000017395.
GeneID	946778.
GenomeReviews	Gene locus JW2294 in contig AP009048_GR. Gene locus b2297 in contig U00096_GR.
KEGG	ecj:JW2294. eco:b2297.
PATRIC	32119965. VBIEscCol129921_2392.
Organism-specific databases
EchoBASE	EB4147.
EcoGene	EG20173. pta.
Phylogenomic databases
eggNOG	COG0857.
GeneTree	EBGT00050000008963.
HOGENOM	HBG576804.
OMA	KPIAQPH.
PhylomeDB	P0A9M8.
ProtClustDB	PRK05632.
Enzyme and pathway databases
BioCyc	EcoCyc:PHOSACETYLTRANS-MONOMER. MetaCyc:PHOSACETYLTRANS-MONOMER.
Gene expression databases
Genevestigator	P0A9M8.
Family and domain databases
InterPro	IPR010766. DRTGG. IPR016475. P-Actrans_bac. IPR004614. P_AcTrfase. IPR002505. PTA_PTB. [Graphical view]
KO	K13788.
Pfam	PF07085. DRTGG. 1 hit. PF01515. PTA_PTB. 1 hit. [Graphical view]
PIRSF	PIRSF006107. PhpActrans_proteobac. 1 hit.
TIGRFAMs	TIGR00651. Pta. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PTA_ECOLI

Accession

Primary (citable) accession number: P0A9M8
Secondary accession number(s): P39184 , P78091, P78189, P78190, Q9EUP2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program