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Reviewed, UniProtKB/Swiss-Prot P43922 (PT1_HAEIN)

Last modified November 3, 2009. Version 65. 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: HI1712
OrganismHaemophilus influenzae [Complete proteome] [HAMAP]
Taxonomic identifier727 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

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Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 – 575575Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147069

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

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Sequences

Sequence LengthMass (Da)Tools
P43922-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: DAC2B7909C38CE73

FASTA57563,691
        10         20         30         40         50         60 
MISGILASPG IAFGKALVLK EEKIVLDTQK ITDDQIDAEV ARFYEGRNAA VEQLNSIRER 

        70         80         90        100        110        120 
ALISLGEEKA AIFEGHLMIL EDEELEEEIL DYLRSNKVNA GVAASKILDQ QVTMLSEIDD 

       130        140        150        160        170        180 
EYLKERAGDI RDIANRLVKN ILGMYIVDLG DIQEESILVA YDLTPSETAQ LNLEKVLGVV 

       190        200        210        220        230        240 
TDIGGRTSHT SIMARSLELP AIVGTNKVTK LVNTGDYLIL DAINNQVYIN PTASQIDELK 

       250        260        270        280        290        300 
ALEAKISEEK AELAKLKDLP AITLDGHKVD VVANIGTIRD CDGAERNGAE GIGLYRTEFL 

       310        320        330        340        350        360 
FMDREQLPTE EEQFIAYKQV VEAMNGRLTV IRTMDIGGDK ELSYLDLPKE MNPFLGWRAI 

       370        380        390        400        410        420 
RIALDRREIL NAQLRAVLRA SAFGKLAVMF PMIISVEEIR ELKAVIETLK AELREEGRLF 

       430        440        450        460        470        480 
DNNIQVGVMV ETPSAAVNAK FLAKEVDFFS IGTNDLTQYT LAVDRGNEFI SHLYNPMHPS 

       490        500        510        520        530        540 
VLGLIKQVID ASHAEGKWTG MCGELAGDER ATLLLLGMGL DEFSMSAISV PRIKKLIRNV 

       550        560        570 
NFQDAKVLAD TALQKPTAAE IDQLIEEFLL ENSLN

« Hide

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Cross-references

Sequence databases

L42023 Genomic DNA. Translation: AAC23357.1.
PIRH64137.
RefSeqNP_439854.1.

3D structure databases

HSSPHSSP built from PDB template 1EZC based on UniProtKB P08839.
ModBaseSearch...

Genome annotation databases

GeneID950872.
GenomeReviewsGene locus HI1712 in contig L42023_GR.
KEGGhin:HI1712.
TIGRHI1712.

Phylogenomic databases

HOGENOMP43922.
OMAEKVSYLY.

Enzyme and pathway databases

BioCycHINF71421:HI_1712-MON.
BRENDA2.7.3.9. 109.

Family and domain databases

InterProIPR008279. PEP_mobile.
IPR018274. PEP_mobile_CS.
IPR006318. PEP_P_trans.
IPR000121. PEP_utilizers.
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.
ProDomPD000940. PEP_utilizers. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01417. PTS_I_fam. 1 hit.
PROSITEPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePT1_HAEIN
AccessionPrimary (citable) accession number: P43922
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 3, 2009
This is version 65 of the entry and version 1 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

Haemophilus influenzae

Haemophilus influenzae (strain Rd): 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