ID A0A1H8TYU7_9GAMM Unreviewed; 756 AA.
AC A0A1H8TYU7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=SAMN04488052_10533 {ECO:0000313|EMBL:SEO96025.1};
OS Aquisalimonas asiatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Aquisalimonas.
OX NCBI_TaxID=406100 {ECO:0000313|EMBL:SEO96025.1, ECO:0000313|Proteomes:UP000199657};
RN [1] {ECO:0000313|EMBL:SEO96025.1, ECO:0000313|Proteomes:UP000199657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6291 {ECO:0000313|EMBL:SEO96025.1,
RC ECO:0000313|Proteomes:UP000199657};
RA de Groot N.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; FOEG01000005; SEO96025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8TYU7; -.
DR STRING; 406100.SAMN04488052_10533; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000199657; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000199657};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..164
FT /note="GAF"
FT /evidence="ECO:0000259|SMART:SM00065"
FT COILED 210..237
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 756 AA; 83065 MW; 0015EA489A234B03 CRC64;
MLQTLHSIIQ EVNAARGLQH ALNIIVKRVA DTTNVDVCSV YLVDQDTQEY VLMATRGLNP
DAVGQVRLRF DEGLVGLVGE RKEPLNLENA EAHPRFRYFP ETGEEKFHSF LGAPIIHFRR
LLGVLVVQQT ARRRFGEEEV AFIVTMAAQL SGAIAHSEAS GGESSGGLPT PLPVTRRALE
GVPGAPGVAF GRAMVAYSPA DLFAVPDRAV EDAESEVAAF RAALKSVRAE VQDLADRLAD
AIPSDEHMMF DVYLKMLDSE SLVDGTEQRI REGNWACGAL RDSIAQYVSV FDEMEDPYLR
ERASDIRDVG RRILMRLQMD SGDTRSVPEG TVLVGEEISA SQLAEIPTER LVGVVTARGS
GNSHVAILAR ALNIPAVMGV AELPVGRLEN KQLIVDGYSG RVHIDPDKRA QKEYRRLLRE
DAELSRDLQT LRNEPAQTPC GFPMGLYANT GLMSDITSSL ASGCDGIGLH RTEFPFMVRE
RFPGEDEQTV VYRQVLEPFV PRPVVLRTLD VGGDKPLPYF PVREENPFLG WRGIRLTLDH
PEIFLTQLRA MLRANADCGN LRILLPMISR VQEVDETRVL LDRAREELAE EGLEVAMPQL
GVMVEVPSAV YQADSLARRV DFLSIGSNDL TQYLLAVDRN NSRVAGLYDE LHPAVLQAVR
QVVEAGERNN CHVSVCGAMA GDPASAILLL GLGVHGLSMS VSSLLKVKWV IRSFTRQQAT
SLLEEALTLE NPADVRRLLN RALEQAGLGG LVRAGK
//
