ID A0A417XV44_9ACTN Unreviewed; 835 AA.
AC A0A417XV44;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE SubName: Full=Phosphoenolpyruvate--protein phosphotransferase {ECO:0000313|EMBL:RHW24047.1};
DE EC=2.7.3.9 {ECO:0000313|EMBL:RHW24047.1};
GN Name=ptsP {ECO:0000313|EMBL:RHW24047.1};
GN ORFNames=D0Z08_26210 {ECO:0000313|EMBL:RHW24047.1};
OS Nocardioides immobilis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2049295 {ECO:0000313|EMBL:RHW24047.1, ECO:0000313|Proteomes:UP000283644};
RN [1] {ECO:0000313|EMBL:RHW24047.1, ECO:0000313|Proteomes:UP000283644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2017083 {ECO:0000313|EMBL:RHW24047.1,
RC ECO:0000313|Proteomes:UP000283644};
RA Li C., Wang G.;
RT "Genome sequencing of Nocardioides immobilis CCTCC AB 2017083 for
RT comparison to Nocardioides silvaticus.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the dihydroxyacetone kinase complex, which is
CC responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation
CC of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is
CC phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent
CC reaction, and a phosphorelay system on histidine residues finally leads
CC to phosphoryl transfer to DhaL and dihydroxyacetone.
CC {ECO:0000256|ARBA:ARBA00002788}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone
CC phosphate + pyruvate; Xref=Rhea:RHEA:18381, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:16016, ChEBI:CHEBI:57642, ChEBI:CHEBI:58702;
CC EC=2.7.1.121; Evidence={ECO:0000256|ARBA:ARBA00001113};
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:RHW24047.1}.
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DR EMBL; QXGH01000036; RHW24047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A417XV44; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000283644; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; IEA:UniProtKB-EC.
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; 3.40.50.510; Phosphotransferase system, mannose-type IIA component; 1.
DR Gene3D; 1.10.274.10; PtsI, HPr-binding domain; 1.
DR InterPro; IPR012844; DhaM_N.
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; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
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; TIGR02364; dha_pts; 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; PF03610; EIIA-man; 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 SUPFAM; SSF53062; PTS system fructose IIA component-like; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Pyruvate {ECO:0000313|EMBL:RHW24047.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000283644};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RHW24047.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..169
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
FT DOMAIN 168..258
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
SQ SEQUENCE 835 AA; 86279 MW; 0B3688CF70FDB446 CRC64;
MTESLSGDSP ISGGQPTVGL VVVSHSRTLA RSAVALAAEM LHGRPLRIEV AAGLDETTFG
TDAVAIMQAI EHADGPAGVV VLMDLGSAVL STELALDLLQ DPSIRDRVTL SPAPLIEGLI
VAAVAAAGGA SRAEVAAEAR DALLGKSGHL SPPPGGTTTD ASDVGTEEIV GVFSVENPHG
LHARPASRLV SEVRALDASV QLRNLTTGGP AVPAGSLSRV ATLAALQGHE VEVRAAGPQA
QEAVEHLLTL AARRFDETVE GAVEPQASSG ATSVSGPLPA SPGIAIGPLR RLTAVPVDLD
QQPVGEPAAE WRRIVESVAA VRRDIEHVRV VTAREVGAEQ ASIFDAHLSL LTDTEMLADV
KTRTSTGIGA VSAWAGCLAE VEREWASLPD PYLRERAADV HAVGDQVLRA LTGEPARRMT
SEGVLVVGDL TPAETASLDL ALVTGVVLAH GSPSSHAVIL ARARDIPVVV AAGAEVLSVP
EGATILLDGS TGELHIDPSP ELLQKYQKRA EDAAGQRARQ LALSEQPAVS RDGTPVAVAA
NLGSVADARA ALAAGADGAG LVRTEFLFLD RSAAPDVDEQ QAEYGAIAAA MDGRPITLRT
LDVGGDKPLA YLPMPQEANP FLGQRGIRLS LAHRDLLRDQ MVAICHTARD HPISIMIPMV
STPGEMIEAR QVLSEAAGPD GLPDGLRIGT MIEVPSAALK IEAFLPYVDF VSIGTNDLTQ
YALAAERGNG AVAALSDALD PGVLQLIDHV CRAAAGRIDV AVCGEAASDE LAIPVLVGLG
VRELSVSPPA VPRVKAAVRE LNVERCAALA RDALTLAGAD EVRKHVLTML SEAPR
//