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Protein

Phosphoenolpyruvate-protein phosphotransferase

Gene

ptsI

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

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

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei186Tele-phosphohistidine intermediateBy similarity1
Binding sitei288PEPBy similarity1
Binding sitei325PEPBy similarity1
Metal bindingi415MagnesiumBy similarity1
Metal bindingi439MagnesiumBy similarity1
Binding sitei449PEPBy similarity1
Active sitei486Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi2.7.3.9. 5998.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate-protein phosphotransferaseBy similarity (EC:2.7.3.9By similarity)
Alternative name(s):
Phosphotransferase system, enzyme IBy similarity
Gene namesi
Name:ptsI
Ordered Locus Names:SCO1391
ORF Names:SC1A8A.11
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001470911 – 556Phosphoenolpyruvate-protein phosphotransferaseAdd BLAST556

Proteomic databases

PRIDEiQ9KZP1.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi100226.SCO1391.

Structurei

3D structure databases

ProteinModelPortaliQ9KZP1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni438 – 439PEP bindingBy similarity2

Domaini

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

Sequence similaritiesi

Belongs to the PEP-utilizing enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105BZ3. Bacteria.
COG1080. LUCA.
HOGENOMiHOG000278513.
InParanoidiQ9KZP1.
KOiK08483.
OMAiNIEIGIM.
OrthoDBiPOG091H00IL.
PhylomeDBiQ9KZP1.

Family and domain databases

Gene3Di1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR024692. PTS_EI.
IPR006318. PTS_EI-like.
IPR008731. PTS_EIN.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000732. PTS_enzyme_I. 1 hit.
SUPFAMiSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
TIGRFAMsiTIGR01417. PTS_I_fam. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9KZP1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METTLRGVGV SHGVAIGEVR HMGTAVLEPP AKQIPAEDAE REQGRARKAV
60 70 80 90 100
EAVAADLMAR GNLAGGEAQA VLEAQAMMAQ DPELLADVER RITVGSTAER
110 120 130 140 150
AVYDAFAAYR ALLAGAGEYL AGRVADLDDV RNRIVARLLG VPMPGVPDSD
160 170 180 190 200
EPYVLIARDL APADTALLDP TLVLGFVTEE GGPTSHSAIL ARALGVPAVV
210 220 230 240 250
ALPGAGEIPE GTVVAVDGST GEIFVNPAEE KKARLAAEAA ERKAALAAAT
260 270 280 290 300
GPGATSDGHK VPLLANIGGP ADVPAAVEAG AEGVGLFRTE FLFLDDSANA
310 320 330 340 350
PSEEKQITAY RQVLEAFPEG RVVVRVLDAG ADKPLDFLTP GDEPNPALGV
360 370 380 390 400
RGLRTLLDHP DVLRTQLTAL AKAAEGLPVY LEVMAPMVAD RADAKAFADA
410 420 430 440 450
CREAGLRAKF GAMVEIPSAA LRARSVLQEV EFLSLGTNDL AQYTFAADRQ
460 470 480 490 500
VGAVSRLQDP WQPALLDLVA LSAEAAKAEG KSCGVCGEAA ADPLLACVLT
510 520 530 540 550
GLGVTSLSMG AASLPYVRAT LAKFTLAQCE RAAAAARAAD SAEEARTAAQ

AVLSGE
Length:556
Mass (Da):57,272
Last modified:October 1, 2000 - v1
Checksum:i7CC6F60B630C7CE7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939108 Genomic DNA. Translation: CAB88887.1.
RefSeqiNP_625674.1. NC_003888.3.
WP_003977434.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB88887; CAB88887; CAB88887.
GeneIDi1096817.
KEGGisco:SCO1391.
PATRICi23732356. VBIStrCoe124346_1399.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939108 Genomic DNA. Translation: CAB88887.1.
RefSeqiNP_625674.1. NC_003888.3.
WP_003977434.1. NC_003888.3.

3D structure databases

ProteinModelPortaliQ9KZP1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO1391.

Proteomic databases

PRIDEiQ9KZP1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB88887; CAB88887; CAB88887.
GeneIDi1096817.
KEGGisco:SCO1391.
PATRICi23732356. VBIStrCoe124346_1399.

Phylogenomic databases

eggNOGiENOG4105BZ3. Bacteria.
COG1080. LUCA.
HOGENOMiHOG000278513.
InParanoidiQ9KZP1.
KOiK08483.
OMAiNIEIGIM.
OrthoDBiPOG091H00IL.
PhylomeDBiQ9KZP1.

Enzyme and pathway databases

BRENDAi2.7.3.9. 5998.

Family and domain databases

Gene3Di1.10.274.10. 1 hit.
3.20.20.60. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR024692. PTS_EI.
IPR006318. PTS_EI-like.
IPR008731. PTS_EIN.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF05524. PEP-utilisers_N. 1 hit.
PF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000732. PTS_enzyme_I. 1 hit.
SUPFAMiSSF47831. SSF47831. 1 hit.
SSF51621. SSF51621. 1 hit.
SSF52009. SSF52009. 1 hit.
TIGRFAMsiTIGR01417. PTS_I_fam. 1 hit.
PROSITEiPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPT1_STRCO
AccessioniPrimary (citable) accession number: Q9KZP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.