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Database: UniProt
Entry: J6UGG4_9RHOB
LinkDB: J6UGG4_9RHOB
Original site: J6UGG4_9RHOB 
ID   J6UGG4_9RHOB            Unreviewed;       755 AA.
AC   J6UGG4;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE            EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN   ORFNames=A33M_1513 {ECO:0000313|EMBL:EJW12951.1};
OS   Rhodovulum sp. PH10.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW12951.1, ECO:0000313|Proteomes:UP000002930};
RN   [1] {ECO:0000313|EMBL:EJW12951.1, ECO:0000313|Proteomes:UP000002930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH10 {ECO:0000313|EMBL:EJW12951.1,
RC   ECO:0000313|Proteomes:UP000002930};
RX   PubMed=23105089; DOI=10.1128/JB.01695-12;
RA   Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT   "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT   Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT   India.";
RL   J. Bacteriol. 194:6363-6363(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJW12951.1}.
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DR   EMBL; AKZI01000019; EJW12951.1; -; Genomic_DNA.
DR   AlphaFoldDB; J6UGG4; -.
DR   STRING; 1187851.A33M_1513; -.
DR   PATRIC; fig|1187851.3.peg.914; -.
DR   eggNOG; COG3605; Bacteria.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000002930; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:UniProtKB-KW.
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   Kinase {ECO:0000313|EMBL:EJW12951.1};
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:UP000002930};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          24..170
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
SQ   SEQUENCE   755 AA;  82807 MW;  89F8B5DE03EF78A5 CRC64;
     MRGALGGPRV LLRRLREVMA EPVSAQERLD KIVVLIAANM VAEVCSCYVL RVDGTLELYA
     TEGLNRQAVH QTVMRADEGL VGLVATEASA INLSDAQAHP AFSYRPETGE EIYRSFLGVP
     ILRAGNTLGV LVVQNRARRT YSEEEVEALQ TTAMVLAEMI ASGELLSLAR PGAEPAVRRP
     VHVTGAALTD GIALGHVVLH EPRVVITNFI ADDVQKELRR LGVAIETLRA ELDLMLESGE
     VAEGGEHRDV LEAYRMFAHD RGWVHKLEEA VLTGLTAEAA VERVQSDTRA RMLRQTDPYL
     RERLHDFDDL AHRLQRQLLG YDHAPTRDKL PEHAVIVARS MGPAALLDYD RNRLRGLVLE
     EGGPNSHVAI VARALGIAAV GEVPNATGLV DPGDGIIVDG ATGDVHVRPS PDMEQAYIER
     VRLRARRQLQ YLSLRDRPSV TRDGHPITLM INAGLPVDLP HIEETGAAGI GLFRTELQFM
     VASQFPRTSE QLALYRNVLD AAGGRPVVFR TLDIGGDKVL PYMRNFEEEN PALGWRAIRL
     GLDRPGLLRS QVRAMLRAAA GRELRVMFPM IAAVDEYDEA KGLVERELTH LRRHGHRLPE
     RVEVGTMLEV PSLLFQLDEL FDRVDFLSVG SNDLLQFMYA ADRGNPRVAS RFDPLSVPVL
     RALKLIVDKA RVHDKPVTLC GELASKPLGA LALIGIGFRA FSVLPSAVGP VKAMLLDLDV
     GKAERLIGQL MALPLGTASI RAKLTAFAEA EGLTL
//
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