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Database: UniProt
Entry: G4E621_9GAMM
LinkDB: G4E621_9GAMM
Original site: G4E621_9GAMM 
ID   G4E621_9GAMM            Unreviewed;       756 AA.
AC   G4E621;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE            EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN   ORFNames=ThisiDRAFT_1750 {ECO:0000313|EMBL:EGZ45644.1};
OS   Thiorhodospira sibirica ATCC 700588.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thiorhodospira.
OX   NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ45644.1};
RN   [1] {ECO:0000313|EMBL:EGZ45644.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ45644.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J.,
RA   Frigaard N.-U., Bryant D., Woyke T.;
RT   "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL   Submitted (SEP-2011) 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}.
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:EGZ45644.1}.
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DR   EMBL; AGFD01000032; EGZ45644.1; -; Genomic_DNA.
DR   RefSeq; WP_006787766.1; NZ_MU255056.1.
DR   AlphaFoldDB; G4E621; -.
DR   STRING; 765914.ThisiDRAFT_1750; -.
DR   PATRIC; fig|765914.3.peg.1736; -.
DR   eggNOG; COG3605; Bacteria.
DR   OrthoDB; 9765468at2; -.
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; IPR023151; PEP_util_CS.
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:SF1; PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM; 1.
DR   PANTHER; PTHR46244; 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.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGZ45644.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          17..164
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
FT   COILED          406..433
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   756 AA;  83391 MW;  CB8FAFFA5791FB15 CRC64;
     MLDVLQRIVL EVNSAENLNQ ALEIIVRRVK LALDIDVCSV YLLLSEENRL VLLASDGLNP
     DSIGRVKLNL GEGLVGVVAR RSEPLNLDNA PDHPAYKYFP ETGEECYHAF LGVPIINARR
     MLGVLVVQQR EERRFRNEHV AFLVTLAAQL AGAISHAEMI GEIGAMQTQA RNAHVQVKGI
     PGSSGIGIGV GVVAYSLADL DAVPDRLPSC IETEVTQFTQ AVEAVQNEME IIKQRMQDSL
     PAEERLLFDA YIMMLGSESL FDRTVQGIRE GNKWAQAALR DTIRENTRSF EEMDDPYLRE
     RASDLRDLGR RILSHLQAPQ RTPEDFPERT ILVGEDLTAT QLAEVPVHRL AGLVSSRGTS
     SSHVAILARA MGVPAVMGMS DLPVTRLEGR QMIVDGYSGR IHIQPGRELL EEFRRLAREE
     RQLSEELRAH SLEPAMTSDG FRIPVYANSG LLADMAPSLQ SGADGIGLYR TEVPFMIRDR
     FPSEDEQTEI YREILTSLDP RPVTLRTLDV GGDKSLPYFP VKEDNPFLGW RGIRITLDHP
     EIFLTQLRAM LRASQGLSNL HIMFPMVSSV SELKGALELL ARARDELLDE QLAILMPKTG
     VMVEVPSAVY QAEALARRVD FLSVGTNDLV QYLLAVDRNN SRVAGIYDCL HPAVLQAMVQ
     AACGAHRAGK TIGVCGEMAA DPAAVLLLLG MEMDSLSVSV SALARVKWVI RHFSRERTQE
     LLEQSLCLDE PAAIRALLNN ALVKAGLGGL VRAGIH
//
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