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Entry: A0A417XV44_9ACTN
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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
//
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