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Reviewed, UniProtKB/Swiss-Prot Q9WXI6 (PT1_BUCAI)

Last modified February 9, 2010. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Phosphoenolpyruvate-protein phosphotransferase
    EC=2.7.3.9
Alternative name(s):
    Phosphotransferase system, enzyme I
Gene names
Name: ptsI
Ordered Locus Names: BU064
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]
Taxonomic identifier118099 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

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Protein attributes

Sequence length571 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr) By similarity.

Catalytic activity

Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.

Cofactor

Magnesium By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Domain

The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity.

Miscellaneous

The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain By similarity.

Sequence similarities

Belongs to the PEP-utilizing enzyme family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 571571Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147061

Sites

Active site1891Tele-phosphohistidine intermediate By similarity
Active site5021Proton donor By similarity
Metal binding4311Magnesium By similarity
Metal binding4551Magnesium By similarity
Binding site2961Substrate By similarity
Binding site3321Substrate By similarity
Binding site4311Substrate By similarity
Binding site4521Substrate; via carbonyl oxygen By similarity
Binding site4531Substrate; via amide nitrogen By similarity
Binding site4541Substrate By similarity
Binding site4551Substrate; via amide nitrogen By similarity

Experimental info

Sequence conflict521Q → H in BAA76879. Ref.1
Sequence conflict611T → P in BAA76879. Ref.1
Sequence conflict5591R → K in BAA76879. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q9WXI6-1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 91927FAE0FD5F276

FASTA57164,386
        10         20         30         40         50         60 
MISGILASPG IAFGTALLLK EDEIVINRKI INIKNITKEI ERFFEGRRKS IQQLTEIKTK 

        70         80         90        100        110        120 
TKEKFGEKKE SIFEGHIMLL EDEELEQEVI SLIKEKNMSA AAATELIIEG QAKALEKLKD 

       130        140        150        160        170        180 
EYLKNRAIDV RDIGNRLLKN ILNLNIIDLN NINNEVILIA KDLTPSETAQ INLKYILGFI 

       190        200        210        220        230        240 
TDLGSRTSHT SIMARSLEIP AIVGTGNITK IVKNNDFIIL DSINNQILIN PSHKLINQTE 

       250        260        270        280        290        300 
VIKKKYLTKK NQLINLKNLQ AITTDGHAIK IGSNIGNVED IKSAKKNGAE CIGLYRTEFL 

       310        320        330        340        350        360 
FMGRNCLPDE NEQFQAYKTI AELMKNKSVI IRTMDIGGDK DLPYMNLPKE ENPFLGWRAI 

       370        380        390        400        410        420 
RISMDRKEIL HTQLNAILRA SAFGKIYILF PMIISVEEIR ILKSEVRKLQ IQLKNNNIPF 

       430        440        450        460        470        480 
DKNIKIGIMI ETPASAIIAE YLIKEVDFFS IGTNDLTQYT LAVDRGNDLI SHLYNPMNPS 

       490        500        510        520        530        540 
VLKLIQQVIN VSHTHGKWTG MCGELAGDER ATILLLGMGL DEFSMSSISI PKIKEIIRKT 

       550        560        570 
SFSSAKKLAQ KALTLPTNRE ILNLVENFVN H

« Hide

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References

« Hide 'large scale' references
[1]"Buchnera sp. DNA for ptsH-ptsI-crr operon."
Matsumoto K., Morioka M., Ishikawa H.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed: 10993077] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tokyo 1998.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB025229 Genomic DNA. Translation: BAA76879.1.
BA000003 Genomic DNA. Translation: BAB12787.1.
RefSeqNP_239901.1.

3D structure databases

SMRQ9WXI6. Positions 2-569.
ModBaseSearch...

Genome annotation databases

GeneID1109471.
GenomeReviewsGene locus BU064 in contig BA000003_GR.
KEGGbuc:BU064.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG456539.
OMAKGIGIGE.
PhylomeDBQ9WXI6.

Enzyme and pathway databases

BioCycBSP107806:BU064-MONOMER.

Family and domain databases

InterProIPR008279. PEP-utiliz_enz_mobile_dom.
IPR006318. PEP_P_trans.
IPR000121. PEP_utilisers.
IPR008731. PTS_PEP_utilis_N.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
[Graphical view]
Gene3DG3DSA:1.10.274.10. PTS_PEP_utilis_N. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PfamPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PRINTSPR01736. PHPHTRNFRASE.
TIGRFAMsTIGR01417. PTS_I_fam. 1 hit.
PROSITEPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePT1_BUCAI
AccessionPrimary (citable) accession number: Q9WXI6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 1, 2000
Last modified: February 9, 2010
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents