SPM_001940
  | Uniprot: A0A037UT59
Description: phosphoenolpyruvate-protein phosphotransferase EC number: 2.7.3.9 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine. {ECO:0000256|PIRNR:PIRNR000732}. Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|PIRNR:PIRNR000732, ECO:0000256|PIRSR:PIRSR000732-3}; Enzyme regulation: Function [CC]: 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). {ECO:0000256|PIRNR:PIRNR000732}. Pathway: Active site: ACT_SITE 190 190 Tele-phosphohistidine intermediate. {ECO:0000256|PIRSR:PIRSR000732-1}.; ACT_SITE 504 504 Proton donor. {ECO:0000256|PIRSR:PIRSR000732-1}. Binding site: BINDING 298 298 Substrate. {ECO:0000256|PIRSR:PIRSR000732-2}.; BINDING 334 334 Substrate. {ECO:0000256|PIRSR:PIRSR000732-2}.; BINDING 433 433 Substrate. {ECO:0000256|PIRSR:PIRSR000732-2}.; BINDING 454 454 Substrate; via carbonyl oxygen. {ECO:0000256|PIRSR:PIRSR000732-2}.; BINDING 455 455 Substrate; via amide nitrogen. {ECO:0000256|PIRSR:PIRSR000732-2}.; BINDING 456 456 Substrate. {ECO:0000256|PIRSR:PIRSR000732-2}.; BINDING 457 457 Substrate; via amide nitrogen. {ECO:0000256|PIRSR:PIRSR000732-2}. Calcium binding: DNA binding: Metal binding: METAL 433 433 Magnesium. {ECO:0000256|PIRSR:PIRSR000732-3}.; METAL 457 457 Magnesium. {ECO:0000256|PIRSR:PIRSR000732-3}. Nucleotide binding: Site: Gene names (primary): Gene names (synonym): Mass: 64,144 Subunit structure [CC]: Gene ontology (GO): cytoplasm [GO:0005737]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]; phosphoenolpyruvate-protein phosphotransferase activity [GO:0008965]; phosphoenolpyruvate-dependent sugar phosphotransferase system [GO:0009401] Gene ontology IDs: GO:0005737; GO:0008965; GO:0009401; GO:0016301; GO:0046872 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000256|PIRNR:PIRNR000732, ECO:0000256|SAAS:SAAS00563041}. Protein families: PEP-utilizing enzyme family Coiled coil: COILED 34 61 {ECO:0000256|SAM:Coils}. Domain [FT]: DOMAIN 6 127 PEP-utilisers_N. {ECO:0000259|Pfam:PF05524}.; DOMAIN 153 226 PEP-utilizers. {ECO:0000259|Pfam:PF00391}.; DOMAIN 255 543 PEP-utilizers_C. {ECO:0000259|Pfam:PF02896}. Motif: Region: EMBL: AGBZ02000001 ProteinModelPortal: MEROPS: EnsemblBacteria KO: KAI92795 UniPathway: CDD: Gene3D: HAMAP: 1.10.274.10;3.20.20.60;3.50.30.10 InterPro: PANTHER: IPR008279;IPR018274;IPR000121;IPR023151;IPR024692;IPR006318;IPR008731;IPR015813 PIRSF: PRINTS: PIRSF000732 PROSITE: Pfam: PS00742;PS00370 ProDom: PF05524;PF00391;PF02896 SMART: SUPFAM: TIGRFAMs: SSF47831;SSF51621;SSF52009 |
354401-356135(-) >nucleotide sequence TTGGCATTCTAATGCTTCTGTCACTAATTGTTCCATTGCCGAAACTTCTAATTTGCTAAT AATTCGACGAGCATTTAAAATACTTGTTGCAGACATTGAAAAGTAATCTAATTTCATTCC CATTAAAAGCGGAATTGCTTGCTCTTCTCCAGCCATTTCGCCACACATTCCAACCCATTT TCCTTCTTTATGGGCACCGTCAATAATTGTTTTAATTAAGCGTAAAACAGATGGATTATA TGGTTGGTATAAATACGCCACAAATTGGCTCATTCGATCAGCTGCCATTGTATATTGAAT TAAATCATTGGTTCCAATTGAAAAGAAATCAGCGTGTTTTGCAAACTGATCAACTAACAT TGCTGCTGCTGGAATTTCCATCATCATTCCAATTTCAATATTATCTGCAACTTTATGTCC TTCTTTAATTAAAGTTGCTTTTTCTTCTAAGGTAATTTTTTTTGCAGCTTTAAATTCATC AATTGTTGCAATCATTGGAAACATAATTCCGATTTTGCCATGAACACTTGCACGTAATAA AGCACGTAATTGTGTTCGGAAAACATCTGTTTTATCTAAACAAAGACGAATTGCACGATA TCCTAAAAATGGGTTCATTTCTTCTGGAAATTTAAAATACGATAATTTTTTATCGCCACC AATATCTAATGTTCGAATAATAACTGGGCGTCCTTGCATTCCTTCTAAGACACCTTTATA AGCTTCATATTGCTCATCTTCAGTTGGGAAATGGTCATTATCCATATATAAGAACTCGCT TCTAAATAAACCAATTCCTTGACCACCATTATCCAAAACACCTTGAACATCTTTTGGCGC TCCAATATTTCCTTCTAAAACAAATTTTTGATATCCATCTTTTGAAACCGTTGGCTTATT TTTAAATGCCAATAATTCTTGTTGTAATTGTAAAAATTTTTCTTTTTCTGCTGTCCAAGT TTTAACCTCTGTTGACATTGGATTTAAGATAACTTCTCCTGTTGTCCCATTAATCATAAC TAATTCATGATGATTTGCTTGTTTCGTAATATCTTTTAATCCTAATACGGCTGGAATTTC TAAACTACGGGCCATAATTGCAGCATGGCTAGTACGCCCTCCCATATCACAACTAAATCC TTTAACAAATTTAGGATTTAACTGTGCTGTTTGTGAAGGTGTTAAATCTTCAGCAACAAT AATAACTTCTTCATGAATAGTTGCTAAATCTAATACCGGAACATTTAAAATATACTTAAT TAAACGATCAGTTACATCTTTAACATCTGCTGCACGTTCTTTAAAATATGGATCATCCAT ACTTGCAAACATTGTAATAAACTTTTGAGCAACAGTATGAATTGCATATGCTGCATTATT GTTATTACTCTTAACAATATTTTTTGCTTCATCAATCATTGCTGGGTCACGCAAAATTTC CTTATGTGCTTCAAAAATTGCTGCTTTTTCTGCCCCTAATTTTTCTAAGGCAATCTTTTG TAGTTTTTCAATATCTGTGTTTGCCTTTTGCATTGCTGCTTCTAGTATTTTAATTTCTTT TGCTGAATCAGAAACCGTATTATTCGAAATTTCATATTTTGGTTCTTCTAACTTAAAAAC TTTGGCAATCGCAATTCCATTACTAGCACCTATCCCATGCAGTTTTTTTGACAT >protein sequence IALEKLGAEKAAIFEAHKEILRDPAMIDEAKNIVKSNNNNAAYAIHTVAQKFITMFASMD DPYFKERAADVKDVTDRLIKYILNVPVLDLATIHEEVIIVAEDLTPSQTAQLNPKFVKGF SCDMGGRTSHAAIMARSLEIPAVLGLKDITKQANHHELVMINGTTGEVILNPMSTEVKTW TAEKEKFLQLQQELLAFKNKPTVSKDGYQKFVLEGNIGAPKDVQGVLDNGGQGIGLFRSE FLYMDNDHFPTEDEQYEAYKGVLEGMQGRPVIIRTLDIGGDKKLSYFKFPEEMNPFLGYR AIRLCLDKTDVFRTQLRALLRASVHGKIGIMFPMIATIDEFKAAKKITLEEKATLIKEGH KVADNIEIGMMMEIPAAAMLVDQFAKHADFFSIGTNDLIQYTMAADRMSQFVAYLYQPYN PSVLRLIKTIIDGAHKEGKWVGMCGEMAGEEQAIPLLMGMKLDYFSMSATSILNARRIIS KLEVSAMEQLVTEALECQTADEVLALVEKSTKNALKA |
© Fisunov Lab of Proteomics, 2016.