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Q9KZP1 (PT1_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. 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:SCO1391
ORF Names:SC1A8A.11
OrganismStreptomyces coelicolor
Taxonomic identifier1902 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length556 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).

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 – 556556Phosphoenolpyruvate-protein phosphotransferase
PRO_0000147091

Sites

Active site1861Tele-phosphohistidine intermediate By similarity
Active site4861Proton donor By similarity
Metal binding4151Magnesium By similarity
Metal binding4391Magnesium By similarity
Binding site2881Substrate By similarity
Binding site3251Substrate By similarity
Binding site4151Substrate By similarity
Binding site4361Substrate; via carbonyl oxygen By similarity
Binding site4371Substrate; via amide nitrogen By similarity
Binding site4381Substrate By similarity
Binding site4391Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KZP1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7CC6F60B630C7CE7

FASTA55657,272
        10         20         30         40         50         60 
METTLRGVGV SHGVAIGEVR HMGTAVLEPP AKQIPAEDAE REQGRARKAV EAVAADLMAR 

        70         80         90        100        110        120 
GNLAGGEAQA VLEAQAMMAQ DPELLADVER RITVGSTAER AVYDAFAAYR ALLAGAGEYL 

       130        140        150        160        170        180 
AGRVADLDDV RNRIVARLLG VPMPGVPDSD EPYVLIARDL APADTALLDP TLVLGFVTEE 

       190        200        210        220        230        240 
GGPTSHSAIL ARALGVPAVV ALPGAGEIPE GTVVAVDGST GEIFVNPAEE KKARLAAEAA 

       250        260        270        280        290        300 
ERKAALAAAT GPGATSDGHK VPLLANIGGP ADVPAAVEAG AEGVGLFRTE FLFLDDSANA 

       310        320        330        340        350        360 
PSEEKQITAY RQVLEAFPEG RVVVRVLDAG ADKPLDFLTP GDEPNPALGV RGLRTLLDHP 

       370        380        390        400        410        420 
DVLRTQLTAL AKAAEGLPVY LEVMAPMVAD RADAKAFADA CREAGLRAKF GAMVEIPSAA 

       430        440        450        460        470        480 
LRARSVLQEV EFLSLGTNDL AQYTFAADRQ VGAVSRLQDP WQPALLDLVA LSAEAAKAEG 

       490        500        510        520        530        540 
KSCGVCGEAA ADPLLACVLT GLGVTSLSMG AASLPYVRAT LAKFTLAQCE RAAAAARAAD 

       550 
SAEEARTAAQ AVLSGE

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL939108 Genomic DNA. Translation: CAB88887.1.
RefSeqNP_625674.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ9KZP1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1096817.
GenomeReviewsGene locus SCO1391 in contig AL645882_GR.
KEGGsco:SCO1391.
NMPDRfig|100226.1.peg.1358.
PATRIC23732356. VBIStrCoe124346_1399.

Phylogenomic databases

HOGENOMHBG456539.
OMAPSEEKQI.
PhylomeDBQ9KZP1.
ProtClustDBCLSK902148.

Enzyme and pathway databases

BRENDA2.7.3.9. 5998.

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.
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_STRCO
AccessionPrimary (citable) accession number: Q9KZP1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 70 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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