ID F5XQ39_MICPN Unreviewed; 863 AA.
AC F5XQ39;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Putative dihydroxyacetone kinase phosphotransferase subunit DhaM {ECO:0000313|EMBL:BAK36870.1};
DE EC=2.7.1.- {ECO:0000313|EMBL:BAK36870.1};
GN Name=dhaM {ECO:0000313|EMBL:BAK36870.1};
GN OrderedLocusNames=MLP_38560 {ECO:0000313|EMBL:BAK36870.1};
OS Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK36870.1, ECO:0000313|Proteomes:UP000007947};
RN [1] {ECO:0000313|EMBL:BAK36870.1, ECO:0000313|Proteomes:UP000007947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA Yamazaki S., Fujita N.;
RT "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL Submitted (MAY-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP012204; BAK36870.1; -; Genomic_DNA.
DR RefSeq; WP_013864712.1; NC_015635.1.
DR AlphaFoldDB; F5XQ39; -.
DR STRING; 1032480.MLP_38560; -.
DR KEGG; mph:MLP_38560; -.
DR eggNOG; COG1080; Bacteria.
DR eggNOG; COG1925; Bacteria.
DR eggNOG; COG3412; Bacteria.
DR HOGENOM; CLU_007308_3_3_11; -.
DR OrthoDB; 9765468at2; -.
DR Proteomes; UP000007947; Chromosome.
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:UniProtKB-KW.
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; 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; 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 Kinase {ECO:0000313|EMBL:BAK36870.1};
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:UP000007947};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAK36870.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..138
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000259|PROSITE:PS51096"
FT DOMAIN 167..257
FT /note="HPr"
FT /evidence="ECO:0000259|PROSITE:PS51350"
SQ SEQUENCE 863 AA; 88038 MW; DF3EEDF86266B85A CRC64;
MVGIVVVSHS RALGEAAVAL AREMVPDATV RIEAAAGLDE TTFGTDAVAI AEAISTAEDG
DGVLVLMDIG SAILSAELAL ELLEDEVRQR VALSPAPLVE GLLAAAVAAA GGASLQQVAT
ESRSGLAGKL TQLGEPRTEA PGSPASGSVV VAPAPALSAA DDEVPPIVRA TFTLTNVHGL
HARPAARLAR LAAGLDADVG IRNLTTGTDW VSARSLSQIA MLGALQGHEL EVSATGPAGQ
AAVDAVLALA RNAFGDPLAA PEAQPLRASS DSRRVASSAR EGVVPDEVPK LLRGLPAAPG
IGIGPAQLLT EQPVEIPERA TGSPTVEQHR LGDALAATAG ELRTLQRRTW DQLGADEADI
FEAHLALLED PELLADVATR IAGGQSAELA WGSATEDIAQ SIAGLEDDYL QTRAADIREL
RGRVLHSLAA LATPIEMTIG SPAEPDPAPS VLIAPDLTAA EAAGLEPTTT LAVALALGSP
TSHASILIRA RGIPLVVAAG PTLLMTPAGS ELAVNGDTGE IQLSPDSATR TVLLDRARRQ
AADRAAAAQS SGRPARTTDG LQILVGANLG SLDDALTAAE SGADLAGLVR TEFLFSGRDT
APDVDEQVEV YRTLAETIGG RRLTLRTLDV GGDKPLSYAP TPAGANPFLG VRGLRLSLAH
PALFRDQLRA IVRVARETSV SIMFPMVSTL TEVHAARRLL DEVIASEGHG TPAGLEVGIM
VEVPAVALKA AEFAAAIDFF SIGTNDLTQY ALAAERGNPD VAAIGDAYDP GVLALIRAVC
QGAAGGPQVA VCGDLAGDPR AAALLVGLGV GTLSVSPPAI PLVKQAVRAV DSGQAEDLAV
TAIAMPGPAE VRALCFDRDE GRQ
//
