ID A0A0P9EB53_9GAMM Unreviewed; 769 AA.
AC A0A0P9EB53;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=SAMN05661077_0984 {ECO:0000313|EMBL:SCX99665.1};
OS Thiohalorhabdus denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalorhabdus.
OX NCBI_TaxID=381306 {ECO:0000313|EMBL:SCX99665.1, ECO:0000313|Proteomes:UP000183104};
RN [1] {ECO:0000313|Proteomes:UP000183104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL 19 {ECO:0000313|Proteomes:UP000183104};
RA Varghese N.;
RL Submitted (OCT-2016) 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; FMUN01000002; SCX99665.1; -; Genomic_DNA.
DR RefSeq; WP_054966519.1; NZ_LJCP01000011.1.
DR AlphaFoldDB; A0A0P9EB53; -.
DR STRING; 381306.AN478_10260; -.
DR PATRIC; fig|381306.5.peg.803; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000183104; 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:SF1; PHOSPHOENOLPYRUVATE-DEPENDENT PHOSPHOTRANSFERASE SYSTEM; 1.
DR PANTHER; PTHR46244; 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.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Reference proteome {ECO:0000313|Proteomes:UP000183104};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SCX99665.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 22..170
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
FT COILED 580..607
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 769 AA; 83507 MW; 283DF897B69FC860 CRC64;
MKPTNVLRTL HRITQEVGRA PNLQQALAIL VSGLRRAMST EVCTVYLSDP EVEGGWVLRA
TDGLNPESVG RVRLGPGEGL VGLVAREEEP VNLDNAGQHP LFRYFPETGE ERFPAFLGVP
ILHRGEVLGV ISVQGTKSER FDEEHATLLF TAAAQLGGVI AHAQVLERLG IRSTAPTEGG
EQEGTPRVEA FLAGQGGAQG ITIGTAWAVY PPADLSAIAD RPCEDPESDK REFQRALNAA
DQEMAELGGN LNERIDEEDA DLIHAYLHIL RDKGFQRRVE ARIDAGTWVQ AAVRDVVWEY
IEAFENMDDP YLRERAADMR DLGRRLIAHL QQGSHRHDGE LPSDTVLVGE EISPLNMASV
PEGHLKGVIS ATGSGGSHVA ILAHAFGIPA VMGVEDLPVA LIDGKRVVVD GYSGRVYVDP
SPKILQEYQR LEAEEAALTE RLAVLRDQSA ESPDGRVIPL YANTGLLADL DPALRSGAEG
IGLYRTELPF LTRDRFPGEA EQIRIYRQVF ETFAPRPVTI RTLDIGGDKL LPYLPIQEDN
PFLGWRGLRL SLDHPEIFLT QLRAILRAAP SGNVRVLLPM VTTVDELDEA LRLIERARKE
LAAVGESAPE LPVGAMIEVP SAVFQTAAIA RRVNFLSIGT NDLTQYLLAV DRNNARVASL
FDSLHPAVLH AIRTVVEEAH GEGRPVSVCG EMAADPVGAL LLAGMGVDDL SMSAGALLRI
KWVLRSFSTT QTRELAELAQ SDECPSSTRT RVEGALLDAG LGSLIRAGD
//