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Protein

Phosphoenolpyruvate-protein phosphotransferase

Gene

ptsI

Organism
Corynebacterium glutamicum (Brevibacterium saccharolyticum)
Status
Unreviewed-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).UniRule annotation

Catalytic activityi

Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.UniRule annotation

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei192Tele-phosphohistidine intermediateUniRule annotation1
Binding sitei295SubstrateUniRule annotation1
Binding sitei331SubstrateUniRule annotation1
Metal bindingi423MagnesiumUniRule annotation1
Binding sitei423SubstrateUniRule annotation1
Binding sitei444Substrate; via carbonyl oxygenUniRule annotation1
Binding sitei445Substrate; via amide nitrogenUniRule annotation1
Binding sitei446SubstrateUniRule annotation1
Metal bindingi447MagnesiumUniRule annotation1
Binding sitei447Substrate; via amide nitrogenUniRule annotation1
Active sitei494Proton donorUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

KinaseUniRule annotation, Transferase

Keywords - Biological processi

Phosphotransferase systemUniRule annotation, Sugar transportUniRule annotation, Transport

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation, PyruvateImported

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoenolpyruvate-protein phosphotransferaseUniRule annotation (EC:2.7.3.9UniRule annotation)
Alternative name(s):
Phosphotransferase system, enzyme IUniRule annotation
Gene namesi
Name:ptsIImported
OrganismiCorynebacterium glutamicum (Brevibacterium saccharolyticum)Imported
Taxonomic identifieri1718 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi196627.cg2117.

Structurei

3D structure databases

ProteinModelPortaliQ93MZ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 129PEP-utilisers_NInterPro annotationAdd BLAST119
Domaini157 – 228PEP-utilizersInterPro annotationAdd BLAST72
Domaini258 – 531PEP-utilizers_CInterPro annotationAdd BLAST274

Sequence similaritiesi

Belongs to the PEP-utilizing enzyme family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiENOG4105BZ3. Bacteria.
COG1080. LUCA.

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.

Q93MZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADVNQDTVL KGTGVVGGVR YASAVWITPR PELPQAGEVV AEENREAEQE
60 70 80 90 100
RFDAAAATVS SRLLERSEAA EGPAAEVLKA TAGMVNDRGW RKAVIKGVKG
110 120 130 140 150
GHPAEYAVVA ATTKFISMFE AAGGLIAERT TDLRDIRDRV IAELRGDEEP
160 170 180 190 200
GLPAVSGQVI LFADDLSPAD TAALDTDLFV GLVTELGGPT SHTAIIARQL
210 220 230 240 250
NVPCIVATGA GIKDIKSGEK VLIDGSLGTI DRNADEAEAT KLVSESLERA
260 270 280 290 300
ARIAEWKGPA QTKDGYRVQL LANVQDGNSA QQAAQTEAEG IGLFRTELCF
310 320 330 340 350
LSATEEPSVD EQAAVYSKVL EAFQESKVVV RSLDAGSDKP VPFASMADEM
360 370 380 390 400
NPALGVRGLR IARGQVDLLT RQLDAIAKAS EELGRGDDAP TLGMAPMVAT
410 420 430 440 450
AYEAKWFADM CRERGLIAGA MIEVPAASLM ADKIMPHLDF VSIGTNDLTQ
460 470 480 490 500
YTMAADRMSP ELAYLTDPWQ PAVLRLIKHT CDEGARFNTP VGVCGEAAAD
510 520 530 540 550
PLLATVLTGL GVNSLSAAST ALAAVGAKLS EVTLETCKKA AEAALDAEGA
560
TEARDAVRAV IDAAV
Length:565
Mass (Da):59,325
Last modified:December 1, 2001 - v1
Checksum:i2C5B4113F600B403
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF392620 Genomic DNA. Translation: AAK76445.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF392620 Genomic DNA. Translation: AAK76445.1.

3D structure databases

ProteinModelPortaliQ93MZ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg2117.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105BZ3. Bacteria.
COG1080. LUCA.

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 nameiQ93MZ3_CORGT
AccessioniPrimary (citable) accession number: Q93MZ3
Entry historyi
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.