ID N1MQQ1_9SPHN Unreviewed; 834 AA.
AC N1MQQ1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=phosphoenolpyruvate--protein phosphotransferase {ECO:0000256|ARBA:ARBA00012232};
DE EC=2.7.3.9 {ECO:0000256|ARBA:ARBA00012232};
GN ORFNames=EBBID32_36170 {ECO:0000313|EMBL:CCW19251.1};
OS Sphingobium indicum BiD32.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW19251.1, ECO:0000313|Proteomes:UP000013201};
RN [1] {ECO:0000313|EMBL:CCW19251.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW19251.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Le V.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW19251.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW19251.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Nielsen J.L., Zhou N.A., Kjeldal H.;
RT "Bisphenol A degrading Sphingobium sp. strain BiD32.";
RL Submitted (APR-2013) 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}.
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:CCW19251.1}.
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DR EMBL; CAVK010000183; CCW19251.1; -; Genomic_DNA.
DR RefSeq; WP_006962442.1; NZ_CAVK010000183.1.
DR AlphaFoldDB; N1MQQ1; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000013201; 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 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:UP000013201};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 22..126
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000259|PROSITE:PS51093"
FT DOMAIN 166..255
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
SQ SEQUENCE 834 AA; 87280 MW; 9D8B344474294405 CRC64;
MGSIILTSPL HGWTTVMDDV PDAVFSGRML GDGIAIDPLA GLLHAPCDGE IMILHASCHA
VTLRGEGGVE VLMHLGIDTV ALGGKGFDPL VTVGDRVARG QPLIRFDLDA VAQSVPSLIT
PIIITNAESF RIQRCVTGQL VGVGEGILYL EPVEAAVALV ATTDGANRAT STLCVPMVHG
IHARPAARIG EAARAFVATS WLVKDGCEAS TRSPIGLLQL GIRLNDQIDI VATGEDAAAA
VAAIRALIES GMDEIEGAGH PVAVQPMLSG SRILPDGALG GTLAAPGYCV GTAHWLRVVD
IDLPRDGQGI DVENQRLNDA IHVMRQRLTQ SGGHDADAAI RRAHAAFLDD PALQHSAFAH
VDAGRDAGHA WRHACRDMAG TMRAMGDARF AERADDLLDL ERQVLHILTG TPDEVPSFPP
GTILLADELV PSQVMALDTH VVGIALEGGG PTSHVAILAA SRGLPMLVAV GRPLFAIADG
TPLILDADDG LILPDPAPET LAAARAKVVR RSQARADAVA SAAMPCVSGD GIRIEAFANL
GSLDDADIAM ANGAEGSGLL RTEFLFLERD CAPDIAEQAA LYGRIAARLD GRPLIIRLLD
IGGDKPASYL PIAAEENPAL GLRGIRVGLA MPDILDRQLR AILSVVPHGQ CRIMVPMVAS
VSELLAVRQR VDALRRELVI DHPVEVGIMV ETPAAAVTAA MLARHADFLS IGTNDLTQYA
LAMDRGNPAV AAGVDGLHPA VLGLIALTTA GASTHKRWVG VCGGLASDRL AIPLLLGLGV
TELSAAPHFV PDLNALVRRL SIAECRRHAE AALQLESADQ VRALARRFEE GLSQ
//
