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O51508 (PT1_BORBU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. 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:BB_0558
OrganismBorrelia burgdorferi (Lyme disease spirochete)
Taxonomic identifier139 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length573 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 – 573573Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147060

Sites

Active site1901Tele-phosphohistidine intermediate By similarity
Active site5041Proton donor By similarity
Metal binding4331Magnesium By similarity
Metal binding4571Magnesium By similarity
Binding site2971Substrate By similarity
Binding site3341Substrate By similarity
Binding site4331Substrate By similarity
Binding site4541Substrate; via carbonyl oxygen By similarity
Binding site4551Substrate; via amide nitrogen By similarity
Binding site4561Substrate By similarity
Binding site4571Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
O51508 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: BB073793270BED45

FASTA57364,595
        10         20         30         40         50         60 
MTLSGKRISK GIGIGEVLCI RKNFDKIISR EKIDFSQVDS EISKFNKAKS KAIEALRDLE 

        70         80         90        100        110        120 
RKAMLQFGDD KKGIFEGQVL IVEDDELDEL VIELIVKENY SAAYSIYLAF ENLVKSVEDY 

       130        140        150        160        170        180 
KDPYLKERAS DYKDIRNRLI SIILGQVSDF SEINKDIILV TEELTPSDTM QFDLNYVKGF 

       190        200        210        220        230        240 
LTAVGGETSH AAILARTMGL PALVMTLSDI DALKDGDKIV IDAMSSIVIK NPSSDEINLY 

       250        260        270        280        290        300 
EGKILRQVEL EKELFSLKDK DAETKDGTKV FLKANIGTPV DITYVNKYGV EGIGLFRTEF 

       310        320        330        340        350        360 
LYMRSLQPPT EDEQFETYKR VIETMEKKGV VTIRTLDVGG DKEIPYLNFK KEENPFLGFR 

       370        380        390        400        410        420 
ALRMYKEYEE LIQAQFNAIF RASHYGKIRV MVPMLTIYEE IETIEYFVNN AKINLKSRGL 

       430        440        450        460        470        480 
PFDENLEVGC MIEVPSAALI SSKLANKLKF FSIGTNDLTQ YVLAVDRGNQ KISNLYDKYN 

       490        500        510        520        530        540 
PAVLKLIKKV LDDGVSSGID VSVCGELGGD DAGALLLVGL GFRSLSMIPS ATLRIKYLLK 

       550        560        570 
KYTIMELEEL ANKVLNSDSK QETLSYFDKF IGD

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000783 Genomic DNA. Translation: AAC66921.1.
PIRE70169.
RefSeqNP_212692.1. NC_001318.1.

3D structure databases

ProteinModelPortalO51508.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBORT00000008968; EBBORP00000008298; EBBORG00000008967.
GeneID1195405.
GenomeReviewsGene locus BB_0558 in contig AE000783_GR.
KEGGbbu:BB0558.
NMPDRfig|224326.1.peg.942.
PATRIC20557747. VBIBorBur75917_0949.
TIGRBB_0558.

Phylogenomic databases

GeneTreeEBGT00050000007069.
HOGENOMHBG456539.
OMAIFRASHY.
PhylomeDBO51508.
ProtClustDBCLSK507663.

Enzyme and pathway databases

BioCycBBUR224326:BB_0558-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_BORBU
AccessionPrimary (citable) accession number: O51508
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: January 25, 2012
This is version 80 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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