ID A0A1W6CVF7_9RHOB Unreviewed; 749 AA.
AC A0A1W6CVF7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=B0A89_03495 {ECO:0000313|EMBL:ARJ68834.1};
OS Paracoccus contaminans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1945662 {ECO:0000313|EMBL:ARJ68834.1, ECO:0000313|Proteomes:UP000193017};
RN [1] {ECO:0000313|EMBL:ARJ68834.1, ECO:0000313|Proteomes:UP000193017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKI 16-01929T\LMG 29738T\CCM 8701T\CIP 111112T
RC {ECO:0000313|Proteomes:UP000193017};
RA Aurass P., Karste S., Trost E., Glaeser S.P., Kaempfer P., Flieger A.;
RT "Genome sequence of Paracoccus contaminans isolated from a water
RT microcosm.";
RL Submitted (MAR-2017) 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; CP020612; ARJ68834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6CVF7; -.
DR STRING; 1945662.B0A89_03495; -.
DR KEGG; pcon:B0A89_03495; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000193017; Chromosome.
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; PF13185; GAF_2; 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 Pyruvate {ECO:0000313|EMBL:ARJ68834.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193017};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ARJ68834.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 25..171
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 749 AA; 81371 MW; 78A5FC7D4597660A CRC64;
MPESLESESR KLLGRLRDTL AAPGDGQARL DRITHHIADS MRSNVCSVYL FRDPDTLELC
ASCGLRPESV HRTRLRLGEG LVGRVARTGR PINTADAPSQ AGFRYMPETG EEVFPSFLGV
PIRRVGERLG VLVVQSREAR EYSEDEIYGL EVVAMVLAEM AELGAFVGNE AHPLTHRFPA
VFRGTGGQEG AAEGQVWLHE PRVVITNPVG DDPAKERARL TEAVAVLRDT VEQMVASAEM
GGGEGEAVLE AYRMFANSRS WLRRMEEDID LGLSAEAAVE KEQSQTRARL ESAADPYLRD
RLHDLDDLSN RLLRILTGQG KDTGGTMPAN PILVARNIGP AELLDYGRSL RGVVLEDGSV
GSHAAVVARA LAIPLVIHAA RIRSEALNGD PILIDGDAGI VHLRPEDSVA AAFRDKIAMQ
AEAQERYAGL RALPATAQCG TTVRLFMNAG LMADLPSIDS SGAEGVGLFR TELQFLTRPR
VPRRSELAGL YARVIENARG KPVVFRTLDI GSDKVLPYMK RLDEPNPAMG WRAIRVGLDK
KGVLQMQLQA LIRASAGRPL NVMFPFIADQ DEFAQGRAML VEQIGREAQM GRPVPAELRV
GAMLETPSLA FAPPAFFRQC DFVSIGGNDL KQFFYAADRE NERVRRRYDT LSTPFLDLIG
MIVDRCGQAG VPLSFCGEDA GRPVEAAVFA ALGLRQLSMR PASIGPVKSL IRRIDLAALR
VAIDAARAEG ATNLRPAVTA FLAASGAQV
//
