Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

20 structures for P08839

Entry ID Method Resolution Chain Position Source
1EZA NMR - A 1-258 PDB
1EZB NMR - A 1-258 PDB
1EZC NMR - A 1-258 PDB
1EZD NMR - A 1-258 PDB
1ZYM X-ray 250 A A/B 1-258 PDB
2EZA NMR - A 1-258 PDB
2EZB NMR - A 1-258 PDB
2EZC NMR - A 1-258 PDB
2HWG X-ray 270 A A/B 1-575 PDB
2KX9 Other - A/B 1-573 PDB
2L5H Other - A/B 1-573 PDB
2MP0 NMR - A 1-258 PDB
2N5T Other - A/B 1-575 PDB
2XDF Other - A/B 1-573 PDB
3EZA NMR - A 1-249 PDB
3EZB NMR - A 1-258 PDB
3EZE NMR - A 1-258 PDB
6V9K X-ray 190 A A/B 261-575 PDB
6VU0 X-ray 350 A A/B 261-575 PDB
AF-P08839-F1 Predicted AlphaFoldDB

No variants for P08839

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P08839

No associated diseases with P08839

6 regional properties for P08839

Type Name Position InterPro Accession
domain PEP-utilising enzyme, C-terminal 250 - 541 IPR000121
domain Phosphotransferase system, enzyme I-like 2 - 566 IPR006318
domain PEP-utilising enzyme, mobile domain 152 - 222 IPR008279
domain Phosphotransferase system, enzyme I N-terminal 4 - 126 IPR008731
active_site PEP-utilising enzyme, active site 184 - 195 IPR018274
conserved_site PEP-utilising enzyme, conserved site 447 - 465 IPR023151

Functions

Description
EC Number 2.7.3.9 Phosphotransferases with a nitrogenous group as acceptor
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

4 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.
kinase activity Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
metal ion binding Binding to a metal ion.
phosphoenolpyruvate-protein phosphotransferase activity Catalysis of the reaction: phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine.

2 GO annotations of biological process

Name Definition
phosphoenolpyruvate-dependent sugar phosphotransferase system The uptake and phosphorylation of specific carbohydrates from the extracellular environment; uptake and phosphorylation are coupled, making the PTS a link between the uptake and metabolism of sugars; phosphoenolpyruvate is the original phosphate donor; phosphoenolpyruvate passes the phosphate via a signal transduction pathway, to enzyme 1 (E1), which in turn passes it on to the histidine protein, HPr; the next step in the system involves sugar-specific membrane-bound complex, enzyme 2 (EII), which transports the sugar into the cell; it includes the sugar permease, which catalyzes the transport reactions; EII is usually divided into three different domains, EIIA, EIIB, and EIIC.
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P77439 fryA Multiphosphoryl transfer protein 1 Escherichia coli (strain K12) PR
10 20 30 40 50 60
MISGILASPG IAFGKALLLK EDEIVIDRKK ISADQVDQEV ERFLSGRAKA SAQLETIKTK
70 80 90 100 110 120
AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA DAAAHEVIEG QASALEELDD
130 140 150 160 170 180
EYLKERAADV RDIGKRLLRN ILGLKIIDLS AIQDEVILVA ADLTPSETAQ LNLKKVLGFI
190 200 210 220 230 240
TDAGGRTSHT SIMARSLELP AIVGTGSVTS QVKNDDYLIL DAVNNQVYVN PTNEVIDKMR
250 260 270 280 290 300
AVQEQVASEK AELAKLKDLP AITLDGHQVE VCANIGTVRD VEGAERNGAE GVGLYRTEFL
310 320 330 340 350 360
FMDRDALPTE EEQFAAYKAV AEACGSQAVI VRTMDIGGDK ELPYMNFPKE ENPFLGWRAI
370 380 390 400 410 420
RIAMDRREIL RDQLRAILRA SAFGKLRIMF PMIISVEEVR ALRKEIEIYK QELRDEGKAF
430 440 450 460 470 480
DESIEIGVMV ETPAAATIAR HLAKEVDFFS IGTNDLTQYT LAVDRGNDMI SHLYQPMSPS
490 500 510 520 530 540
VLNLIKQVID ASHAEGKWTG MCGELAGDER ATLLLLGMGL DEFSMSAISI PRIKKIIRNT
550 560 570
NFEDAKVLAE QALAQPTTDE LMTLVNKFIE EKTIC