ID A0A1I0C6W0_9RHOB Unreviewed; 748 AA.
AC A0A1I0C6W0;
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=SAMN04489858_103174 {ECO:0000313|EMBL:SET14506.1};
OS Paracoccus homiensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=364199 {ECO:0000313|EMBL:SET14506.1, ECO:0000313|Proteomes:UP000199180};
RN [1] {ECO:0000313|EMBL:SET14506.1, ECO:0000313|Proteomes:UP000199180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17862 {ECO:0000313|EMBL:SET14506.1,
RC ECO:0000313|Proteomes:UP000199180};
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; FOHO01000003; SET14506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0C6W0; -.
DR STRING; 364199.SAMN04489858_103174; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000199180; 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:UP000199180};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SET14506.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 25..171
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 748 AA; 83320 MW; 3AC9CA163A59D1FE CRC64;
MHDRKDSDSR KLLRRLKEIL AAAGGGQDRL DQITHHIADS MGTDVCSIYL FRDPQTLELC
ATEGLRAEAV HQTRLRLGEG LVGRVARAGR NINTENAPAE PGFRFMPETG EEVFPSFLGV
PIQRVGEKLG VLVVQCREAR LFSDDEIYGL EVVAMVLAEM TELGAFQGSQ SDSMPQAHRF
PLMLRGTTAQ EGAAEGHVWL HEPRVVVANP VGDDPEKERA RLHEGVAMLR ESVDRMVGAA
DMGGTGDHTE ILETYRMFAH SRSWLKRMEE DIRLGLSAEA AVEKEQSSAR ARMEMSADPY
LRDRLHDLDD LSNRLLRILT GQGRDTGAEM PERPILIARN IGPAELLEYG RKLKGVVLEE
GSVGSHAAVV ARALTIPLVI HASRITTEAL NGDPILIDGD QGIVHLRPEE TVATAFRDKI
AMQAEAQNRY ASLRNLPATA TCGTTVQLYM NAGLMADLPS LEGSGAEGVG LFRTELQFLI
RNHVPRRGEL AQLYRRVIDN SHGKPVMFRT LDIGSDKVLP YMKPQDEPNP AMGWRAIRVG
LDKRGVLRMQ LQALIRASVG RPLHVMFPFI ADISEYEDAY RILMQEMSRE QRLGHEMPTD
IRVGAMLETP SLAFAPQRFF EMCDFVSIGG NDLKQFFFAA DRENERVRRR YDTLNTSFLA
LLEQIIARCE AARVPLSFCG EDAGRPVEAL TFAALGLRRL SMRPASIGPV KHLIRRVSIA
ELRQVIEDGK SQGLTNLRRP ITEWLARQ
//
