ID Q1PXY6_KUEST Unreviewed; 678 AA.
AC Q1PXY6;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN Name=ptsI {ECO:0000313|EMBL:CAJ72907.1};
GN ORFNames=KsCSTR_03250 {ECO:0000313|EMBL:QII09704.1}, KSMBR1_1887
GN {ECO:0000313|EMBL:SOH04386.1}, kustd2162
GN {ECO:0000313|EMBL:CAJ72907.1};
OS Kuenenia stuttgartiensis.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Kuenenia.
OX NCBI_TaxID=174633 {ECO:0000313|EMBL:CAJ72907.1};
RN [1] {ECO:0000313|EMBL:CAJ72907.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16598256; DOI=10.1038/nature04647;
RA Strous M., Pelletier E., Mangenot S., Rattei T., Lehner A., Taylor M.W.,
RA Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., Fonknechten N.,
RA Vallenet D., Segurens B., Schenowitz-Truong C., Medigue C., Collingro A.,
RA Snel B., Dutilh B.E., OpDenCamp H.J.M., vanDerDrift C., Cirpus I.,
RA vanDePas-Schoonen K.T., Harhangi H.R., vanNiftrik L., Schmid M.,
RA Keltjens J., vanDeVossenberg J., Kartal B., Meier H., Frishman D.,
RA Huynen M.A., Mewes H., Weissenbach J., Jetten M.S.M., Wagner M.,
RA LePaslier D.;
RT "Deciphering the evolution and metabolism of an anammox bacterium from a
RT community genome.";
RL Nature 440:790-794(2006).
RN [2] {ECO:0000313|EMBL:CAJ72907.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SOH04386.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kuenenia_mbr1_ru-nijmegen {ECO:0000313|EMBL:SOH04386.1};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000221734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Frank J.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QII09704.1, ECO:0000313|Proteomes:UP000501926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSTR1 {ECO:0000313|EMBL:QII09704.1,
RC ECO:0000313|Proteomes:UP000501926};
RA Ding C., Adrian L.;
RT "Newly sequenced genome of strain CSTR1 showed variability in Candidatus
RT Kuenenia stuttgartiensis genomes.";
RL Submitted (FEB-2020) 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; CT573072; CAJ72907.1; -; Genomic_DNA.
DR EMBL; CP049055; QII09704.1; -; Genomic_DNA.
DR EMBL; LT934425; SOH04386.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1PXY6; -.
DR KEGG; kst:KSMBR1_1887; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000221734; Chromosome Kuenenia_stuttgartiensis_MBR1.
DR Proteomes; UP000501926; 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 CDD; cd00367; PTS-HPr_like; 1.
DR Gene3D; 3.30.1340.10; HPr-like; 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; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_sf.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
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; IPR001020; PTS_HPr_His_P_site.
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; TIGR01003; PTS_HPr_family; 1.
DR NCBIfam; TIGR01417; PTS_I_fam; 1.
DR PANTHER; PTHR46244; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR46244:SF3; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; 1.
DR Pfam; PF05524; PEP-utilisers_N; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF00381; PTS-HPr; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SUPFAM; SSF47831; Enzyme I of the PEP:sugar phosphotransferase system HPr-binding (sub)domain; 1.
DR SUPFAM; SSF55594; HPr-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 1.
DR PROSITE; PS00369; PTS_HPR_HIS; 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:CAJ72907.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000221734};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAJ72907.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 10..97
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
FT COILED 235..262
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 678 AA; 76255 MW; 58146E1A6E590B4B CRC64;
MDFFFVNSKI SERKVKIWNS NGLHARPATK FSEIANKYTS EIRVEAKGKN IDGKSIIELL
TLGAENGTEL LISAKGVDCA EALDALEELV NSKFEEEFME IRKGIAVSPG VVIRQAFLFE
SEGFRIPRHV IKNEAVEDEV CRLEKAIDAS KKEIEDLEKK VSENLGSEIG SIFGTHRMVL
QDARLKDEII KRIRKTNFTP EFAVSLALRV YIRKFQDIKD SYLAERVTDI FDVERRLLRN
LLGEKREELK NLEEEVVLVA HDLTPSQTAM LDPQKVKGFA TDGGGRTSHT AIVARALGIP
AVVGLGTVTS DVFGGDIVIV DGNRGLVIVR PDDETLATYQ SKVKSIDVFE KKLAIELKDQ
PSTTADGRHI SIFGNIEFPR EIGVNLNYGA EGIGLYRTEF LYLNSPTPPT EEQHLEAYTT
VVQELKGRPV IIRTLDLGAD KLPYLEHRKE GNPFLGCRSI RYCFENPSIF KIQLRALLRA
SALGEVKILF PLISSIQELR RAKQMVYETM EDLDKENISF DKNVKMGTML EVPSSVMISD
MLAKECDFFS IGTNDLIQYS LAVDRNNERV AYLYCPVHPA ILRFLKFAIK SAHENDIPVG
ICGEMGGELE YTIPLVGLGL KEFSVAPATI IPEMKKIIRS VSFEEAREVA ETVFKFDNPE
KTKKYLNDFV RKILPEVY
//
