ID Q2G5M4_NOVAD Unreviewed; 836 AA.
AC Q2G5M4;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN OrderedLocusNames=Saro_2413 {ECO:0000313|EMBL:ABD26849.1};
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD26849.1, ECO:0000313|Proteomes:UP000009134};
RN [1] {ECO:0000313|Proteomes:UP000009134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC / F199 {ECO:0000313|Proteomes:UP000009134};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL Submitted (JAN-2006) 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; CP000248; ABD26849.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2G5M4; -.
DR STRING; 279238.Saro_2413; -.
DR KEGG; nar:Saro_2413; -.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_007308_3_3_5; -.
DR Proteomes; UP000009134; 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; 2.70.70.10; Glucose Permease (Domain IIA); 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; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_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; IPR001127; PTS_EIIA_1_perm.
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; TIGR00830; PTBA; 1.
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 Pfam; PF00358; PTS_EIIA_1; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR PRINTS; PR01736; PHPHTRNFRASE.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
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; PS51093; PTS_EIIA_TYPE_1; 1.
DR PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 1.
DR PROSITE; PS00369; PTS_HPR_HIS; 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 Reference proteome {ECO:0000313|Proteomes:UP000009134};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABD26849.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 23..127
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000259|PROSITE:PS51093"
FT DOMAIN 168..255
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
FT REGION 256..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 86310 MW; 9A68E2C52B918D88 CRC64;
MMGSIVLSAP IAGWVSALDE VPDGVFSARL LGDGVAIDPV EGLLCAPCDG EILSVHAARH
AVTMAGEGGV ELLMHLGIDT VELKGDGFET LVRAGHRVVR GQPLLRFSLD DLAGRAPSLV
SPVIVTNGDR FTISSCTVDA LVAVGDDLIR LDPVGVAPSP DRAPVGEAVG AIVVVPLPNG
LHARPAARLG EAARAFAAET RIVKNGRAVS TRSPVGLLGL SIQLGDEILV EASGPDASQA
VAALVDLIRS GLGEGAEHDA AAEPRASSAG MPPFAPVPDG ALRGNLASPG FALGTCHRLD
RSEPELPVQG KGKEEERIRL LSAMDHLRSR LAISSEVSPK AAICSAHRAL LDDPELEAAA
LSRIAEGEDA AHAWREACRA SAVVLRGSGS ARFAERADDV LDLGRQLVTI LIGELDETLA
FPPGTILLAD ELLPSQIMQL GAEVTGIALA NGGPTSHVAI LAASMGIPML VAIGDALAGV
RAGDKAILDA DGGFLLPAPG AAALAEAEAE VAARQARRAD ALASASELCH SRDGARIEVF
ANLGSLDDAR RAVSAGAEGC GLLRTEFLFL ERESAPTVAQ QAELYAGIAD ALGGRPLIVR
LLDIGGDKPA TYLPIAPEAN PALGLRGIRV GLAHPDVLED QLRAILSVER GGALRIMVPM
VTGVAEVREV RQRVDRISAE LGLAQRVEVG IMVETPAAAA TAFLLAPHAD FMSIGTNDLT
QYVLAMDRDN PAVAGGIDGL HPAVLNLIAQ TVRGAQSVGR WTGVCGGLAA DRLAVPLLLG
LGVTELSVPL RQLPEIKALV RGLSISDCKT LALEALQLES AAEIRALSRA FVETLP
//
