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Q89B04 (PT1_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:bbp_060
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 576576Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147063

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

Sequences

Sequence LengthMass (Da)Tools
Q89B04 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 546C4EF1BF9E99CA

FASTA57665,449
        10         20         30         40         50         60 
MISGILASPG ITFGKALLLK NEILSINYKK ISNQDIHQEV KKFINGKNKT ICQLQEIKNK 

        70         80         90        100        110        120 
TQQKFENTQS NIFEGHIMLL EDDEFQQKII SLIQDRNISS EYATKIIIEE HAKTLEQLND 

       130        140        150        160        170        180 
EYLKNRAIDI QDIGNRLLKN ILNIDIKDLN NIKNPVILIA RDLTPSETAQ INLKKVLGFI 

       190        200        210        220        230        240 
TDLGGQTSHT SIIARSLELP AIVGTKNITE KAKNDDFIIL DSINNKISIN PSLEEIHRIK 

       250        260        270        280        290        300 
QKKKKYESEK KLLIESKNLY AITKDKHKVE IGANISTIQD INNAKKYGAE CIGLYRTEFL 

       310        320        330        340        350        360 
FMNRNYLPSE EEQFNTYKTI AEEMKNKSII IRTMDVGGDK NISYMNIPKE ENPFLGWRAI 

       370        380        390        400        410        420 
RIAIDRKEIL HAQLKAILRA SAFGKLRIMF PMIISVEEVR TLQYELEKLK QLLHHQKIPF 

       430        440        450        460        470        480 
NAKIEVGIMI ETPASAIIAH HLAQEVDFFS IGSNDLTQYT LAVDRGNDLI SHLYNPMSPS 

       490        500        510        520        530        540 
VLSLIQQVIN ASHKVGKWTG MCGELAGDEK ATLLLLGMGL DEFSMSAATI PKIKKIIRES 

       550        560        570 
TFLDVKKLAK KVLLQPTYNE VNNTINTFIN INNKNK

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016826 Genomic DNA. Translation: AAO26799.1.
RefSeqNP_777694.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89B04.
SMRQ89B04. Positions 2-569.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000002338; EBBUCP00000002162; EBBUCG00000002338.
GeneID1058192.
GenomeReviewsGene locus bbp_060 in contig AE016826_GR.
KEGGbab:bbp060.
PATRIC21244893. VBIBucAph80364_0057.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000007917.
HOGENOMHBG456539.
OMAVRKANIV.
PhylomeDBQ89B04.
ProtClustDBPRK11177.

Enzyme and pathway databases

BioCycBAPH224915:BBP_060-MONOMER.

Family and domain databases

InterProIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR006318. PEP_util_enz.
IPR024692. PTS_enz_I.
IPR008731. PTS_PEP_utilis_N.
IPR015813. Pyrv/PenolPyrv_Kinase.
[Graphical view]
Gene3DG3DSA:3.50.30.10. PEP_mobile. 1 hit.
G3DSA:1.10.274.10. PTS_PEP_utilis_N. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KOK08483.
PANTHERPTHR22931:SF10. PTHR22931:SF10. 1 hit.
PfamPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFPIRSF000732. PTS_enzyme_I. 1 hit.
PRINTSPR01736. PHPHTRNFRASE.
SUPFAMSSF47831. PEP-utilisers_N. 1 hit.
SSF52009. PEP_mobile. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR01417. PTS_I_fam. 1 hit.
PROSITEPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePT1_BUCBP
AccessionPrimary (citable) accession number: Q89B04
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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