ID A0A1H3Z6G5_9RHOB Unreviewed; 747 AA.
AC A0A1H3Z6G5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=SAMN05444370_103417 {ECO:0000313|EMBL:SEA19403.1};
OS Rubrimonas cliftonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rubrimonas.
OX NCBI_TaxID=89524 {ECO:0000313|EMBL:SEA19403.1, ECO:0000313|Proteomes:UP000198703};
RN [1] {ECO:0000313|EMBL:SEA19403.1, ECO:0000313|Proteomes:UP000198703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15345 {ECO:0000313|EMBL:SEA19403.1,
RC ECO:0000313|Proteomes:UP000198703};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-
CC L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA-
CC COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000683};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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DR EMBL; FNQM01000003; SEA19403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3Z6G5; -.
DR STRING; 89524.SAMN05444370_103417; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000198703; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008965; F:phosphoenolpyruvate-protein phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR006318; PTS_EI-like.
DR InterPro; IPR008731; PTS_EIN.
DR InterPro; IPR036618; PtsI_HPr-bd_sf.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01417; PTS_I_fam; 1.
DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SMART; SM00065; GAF; 1.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Reference proteome {ECO:0000313|Proteomes:UP000198703};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SEA19403.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 25..171
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 747 AA; 81053 MW; 8B7FF5DC16E5D0BC CRC64;
MTPSAGVGSR AMLRRLRQVM AEPGDGQQRL DKITQVIATN MVAEVCSIYL RREPGMLELF
ATEGLRKDAV HKAALRIGEG LVGRIAERAT PIATDNAPAA PGFQYLPETG EEVYRSFCGV
PIQRLGKVLG VLVVQNTTQR TYDEDEVDAL EVVAMVIAEM AESGALSAGR EIERGKRGPL
TARGVSAADG AAVGHVHLHD PRIAIANPIV DDVPRERERL RGAMVALQGE VDRLLDTDLL
KGGGEHRDVL ETYRMFAHDK GWLRRLDEAV ASGVVAEVAV ERVQSAARAR MDRVADPYLR
ERLHDLDDLA NRLLRLLTGA EATPPPEDAI LVARSIGPAE LLELAGRVRG VVMEEGSAGG
HAAIVARALG VPMIVQAHGV VAEAENGDRA IVDGDEGVAH FRPDATVLDA FGERLALEAE
TQALYRSLRD LPAQTRDGVC VSLMMNAGLA TDMPSLAESG AEGVGLYRTE LMFMVRATMP
GRDAQEAVYR RILDEAAGRR VVFRTLDIGS DKILPYMRRT EEDNPAMGWR ALRFGLDRPR
LMTMQLQALL RGAAGRPLSV MFPFVTTLEE FRKARALLLR ERDRQAARGR PAPERLEIGA
MLETPAMAHA PDAFFREADF ISVGGNDLKQ FFFAADRGNE RVRRRYDTLS PPYLAFLKRI
VGRCAENGAS LSFCGESAGR PIEALALAAI GFRAFSMRPS AIGMVKRALR AVDLSEAEAL
VAAAVAGGDP TARPALTRYA QDCGVSI
//
