ID A0A285CNW6_9RHOB Unreviewed; 747 AA.
AC A0A285CNW6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=SAMN05878503_10392 {ECO:0000313|EMBL:SNX69105.1};
OS Cereibacter ovatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cereibacter.
OX NCBI_TaxID=439529 {ECO:0000313|EMBL:SNX69105.1, ECO:0000313|Proteomes:UP000219467};
RN [1] {ECO:0000313|EMBL:SNX69105.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA234 {ECO:0000313|EMBL:SNX69105.1};
RA de Groot N.N.;
RL Submitted (AUG-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; OAOQ01000003; SNX69105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285CNW6; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000219467; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000219467};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SNX69105.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 25..171
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
SQ SEQUENCE 747 AA; 82332 MW; 0DDFA735E7871A42 CRC64;
MPERSESESR KLLRRLRDSL ALSGAGQDRL DRITALIADS MRTEVCSIYL FRDAETLELS
ATQGLKPEAV HKTRLKLGEG LVGRVARTAT PINTGNAPSE RGFRFMPETG EEVFSSFLGV
PIQRVGEKLG VLVVQSRDER EYSDDEVYAL EVVAMVLAEM AELGAFTGEG EALSAKHTQP
VLFRGGCGQE GAAEGHVWLH EARVVVTNPV ADDPERELDR IRAAVAQLRV SVDDLMSAST
LDKEQRQVLE AYRLFAHSRG WLRRMEEDIM AGLSAEAAVQ KEQSAARARL EQVPDAYLRD
RLHDLDDLSH RLLRILTGQG RDTGAAMPEN PVLVARNIGP AELLEYGRKL RGVVLEEGSV
GSHAAIVARA LAIPLVIHAE RITTEALNGD HIMLDGDAGV VHLRPEATVA AAFRDKMAMM
AKAQERYASL RNLPAQSKCG TVTGILMNAG LMADLPSLDS SGAEGVGLFR TELQFLIRNQ
MPKRDELARL YARVMDAARG HRVIFRTLDI GSDKVLPYLK PHDEPNPAMG WRAIRVGLDK
PGVLRMQLQA LIRAAAGRDL CIMFPFVSEH HEFMMARSHL LRELHRERSL GHPVPTNISV
GTMLETPSLA YAPRAFFEMT DFVSIGGNDL KQFFFAADRE NERVRRRYDV LNVSFLSFLE
HVIARCAETG TPLSFCGEDA GRPIEALCFA ALGIRSLSMR PASVGPVKAL LRRVDLSDAR
AVIEMARASG AETVRPAILE WLATQVD
//
