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Database: UniProt
Entry: B8GLD7_THISH
LinkDB: B8GLD7_THISH
Original site: B8GLD7_THISH 
ID   B8GLD7_THISH            Unreviewed;       756 AA.
AC   B8GLD7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE            EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN   OrderedLocusNames=Tgr7_2414 {ECO:0000313|EMBL:ACL73492.1};
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL73492.1, ECO:0000313|Proteomes:UP000002383};
RN   [1] {ECO:0000313|EMBL:ACL73492.1, ECO:0000313|Proteomes:UP000002383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL73492.1,
RC   ECO:0000313|Proteomes:UP000002383};
RX   PubMed=21475584;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL73492.1; -; Genomic_DNA.
DR   RefSeq; WP_012638967.1; NC_011901.1.
DR   AlphaFoldDB; B8GLD7; -.
DR   STRING; 396588.Tgr7_2414; -.
DR   KEGG; tgr:Tgr7_2414; -.
DR   eggNOG; COG3605; Bacteria.
DR   HOGENOM; CLU_007308_7_1_6; -.
DR   OrthoDB; 9765468at2; -.
DR   Proteomes; UP000002383; 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; 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   Pyruvate {ECO:0000313|EMBL:ACL73492.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002383};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACL73492.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          17..164
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
FT   COILED          209..236
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   756 AA;  83263 MW;  D01CE22516F57CD7 CRC64;
     MLDILRRIVQ EVSTAEDLHQ ALDIIVHRVK QALGIDVCSV YLMAPDRQHL MLMATEGLNP
     DSVGHVRLAL GEGLVGLVAE RAEPVNLDNA TDHPLFRYFP ETGEERYHAF LGVPIVHHRR
     MLGVLVAQQH ERRRFDDEHV ALLITLAAQL AGAISHAELI GEVGPRRGTP RQANLQIMGI
     PGASGVAIGT AVVAYAAAAL DSVPDREPVV SVEEEIHAFR EAVQRVREEM ESIKLRMNGV
     LSSEELLLFD AYVMMLGSDS LVLRTIERIE AGSWAQAALR DTIRESTRAF DDMDDPYLRE
     RATDLRDIGR RILTHLQSGQ RKTEDFPERT ILIGEDLTAT QLAEVPVERL AGLVSARGTG
     SSHVAILARA MGIPAVMGVS DLPVGRMDGM EVVIDGYRGQ IFLQPSRELR EEFQRLVDEE
     RELAEGLRNL ALEPATTQDG VVIPVYANSG LLADINPSKQ SGADGIGLYR TEVPFMIRDR
     FPGEEEQVEI YRQILSSFDP RPVTLRTLDV GGDKALPYFP VHEDNPFLGW RGIRITLDHP
     EIFLTQLRAM LRASQGLSNL QILFPMISSL DELKGALRLL QRARDELLDE HYVIPMPKVG
     VMVEVPSAVY LAEALARRVD FLSVGSNDLV QYLLAVDRNN ARVADLYNAL HPAVLRALKQ
     VSEGAKKAGK PVSICGEMAA DPAAAILLIG MGIDSLSVNV ASLARVKWVI RSFSQARARE
     LLNQCMEMEE PAAIRALLNN ALMQVGLGGL VRAGKT
//
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