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Database: UniProt
Entry: T0I609_9SPHN
LinkDB: T0I609_9SPHN
Original site: T0I609_9SPHN 
ID   T0I609_9SPHN            Unreviewed;       739 AA.
AC   T0I609;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE            EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN   ORFNames=L288_10065 {ECO:0000313|EMBL:EQB07100.1};
OS   Sphingobium quisquiliarum P25.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1329909 {ECO:0000313|EMBL:EQB07100.1, ECO:0000313|Proteomes:UP000015525};
RN   [1] {ECO:0000313|EMBL:EQB07100.1, ECO:0000313|Proteomes:UP000015525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P25 {ECO:0000313|EMBL:EQB07100.1,
RC   ECO:0000313|Proteomes:UP000015525};
RX   PubMed=24029763;
RA   Kumar Singh A., Sangwan N., Sharma A., Gupta V., Khurana J.P., Lal R.;
RT   "Draft Genome Sequence of Sphingobium quisquiliarum Strain P25T, a Novel
RT   Hexachlorocyclohexane (HCH)-Degrading Bacterium Isolated from an HCH
RT   Dumpsite.";
RL   Genome Announc. 1:e00717-13(2013).
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:EQB07100.1}.
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DR   EMBL; ATHO01000085; EQB07100.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0I609; -.
DR   PATRIC; fig|1329909.3.peg.1936; -.
DR   Proteomes; UP000015525; 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; 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; 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.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 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   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          6..151
FT                   /note="GAF"
FT                   /evidence="ECO:0000259|SMART:SM00065"
SQ   SEQUENCE   739 AA;  82089 MW;  93558B8CF9B6E56F CRC64;
     MAARNSAQAK LNKVVDIIGQ ALSSEVCSIY LVREGLLELF ATRGLKQEAV HVTRMAMGEG
     LVGLIATNVE TLNLDEAASH PDYSYRPETG EELFHSFAGV PIVRRERAIG VLCVQHVEPR
     RYEEVEIEAL QTVAMVLSEL IANAELADDG PADSRVQDTG TIMLQGLQLV MGMARGHAVF
     HQPRVHVEHT VAEDTEAERQ RVISAFAKMR EQIDRMTGTA EFGTEGEHQE VLETYKMFAY
     DEGWIRRINE AIDSGLTAEA AIERVQQRTR MRMRQIDDPL LQDRMHDLED LANRLLRIVS
     GQLGTAAQLG LRQDAILIAR NLGPAELLEY DRRRLKGVIL EEGSLTAHVT IVARAMGVPV
     LGRVREIRHK VNEGDLILMD VGSNSLLIRP TADMDEAFEN KLHVTQKRRA EFAAMRDLPS
     VTTDGQRIEL MVNAGLREDA QALDLVGADG IGLFRTEFQF LVSATLPQRE KQQRLYKDVL
     DAAGDRPVIF RTVDIGGDKA LPYMTRDGDD ELEDNPAMGW RALRLALDRD GLMKAQARAL
     LEAAAGKVLN IMFPMVSEPW EYEQARALVE HQRAWLLSQR KKVPVAVRYG AMLEVPALAE
     VLDLLLPKLD FLSIGTNDLT QFLFAADRAH PKLAERYDWL SIAILRFLDR VVRTCAAYEC
     PVGVCGEMGG RTLEAMALIG LGVRRLSITP ASVGPVKAMI RAIDAAELQA LMRSLLDEGA
     VDLRARLAGW ASERGIELN
//
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