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Database: UniProt
Entry: A0A120I0X4_9MICO
LinkDB: A0A120I0X4_9MICO
Original site: A0A120I0X4_9MICO 
ID   A0A120I0X4_9MICO        Unreviewed;       231 AA.
AC   A0A120I0X4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=phosphoenolpyruvate--glycerone phosphotransferase {ECO:0000256|ARBA:ARBA00012095};
DE            EC=2.7.1.121 {ECO:0000256|ARBA:ARBA00012095};
GN   ORFNames=AWU67_06300 {ECO:0000313|EMBL:AMB58532.1};
OS   Microterricola viridarii.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microterricola.
OX   NCBI_TaxID=412690 {ECO:0000313|EMBL:AMB58532.1, ECO:0000313|Proteomes:UP000058305};
RN   [1] {ECO:0000313|EMBL:AMB58532.1, ECO:0000313|Proteomes:UP000058305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS5:02 {ECO:0000313|EMBL:AMB58532.1,
RC   ECO:0000313|Proteomes:UP000058305};
RX   PubMed=26854947; DOI=10.1016/j.jbiotec.2016.02.011;
RA   Himanshu, Swarnkar M.K., Singh D., Kumar R.;
RT   "First complete genome sequence of a species in the genus Microterricola,
RT   an extremophilic cold active enzyme producing bacterial strain ERGS5:02
RT   isolated from Sikkim Himalaya.";
RL   J. Biotechnol. 222:17-18(2016).
RN   [2] {ECO:0000313|Proteomes:UP000058305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS5:02 {ECO:0000313|Proteomes:UP000058305};
RA   Kumar R., Singh D., Swarnkar M.K.;
RT   "First complete genome sequence of a species in the genus Microterricola,
RT   an extremophilic cold active enzyme producing strain ERGS5:02 isolated from
RT   Sikkim Himalaya.";
RL   Submitted (JAN-2016) 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=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};
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DR   EMBL; CP014145; AMB58532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A120I0X4; -.
DR   KEGG; mvd:AWU67_06300; -.
DR   Proteomes; UP000058305; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   CDD; cd00367; PTS-HPr_like; 1.
DR   Gene3D; 3.30.1340.10; HPr-like; 1.
DR   Gene3D; 3.40.50.510; Phosphotransferase system, mannose-type IIA component; 1.
DR   InterPro; IPR039643; DhaM.
DR   InterPro; IPR012844; DhaM_N.
DR   InterPro; IPR000032; HPr-like.
DR   InterPro; IPR035895; HPr-like_sf.
DR   InterPro; IPR004701; PTS_EIIA_man-typ.
DR   InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR   InterPro; IPR001020; PTS_HPr_His_P_site.
DR   NCBIfam; TIGR02364; dha_pts; 1.
DR   NCBIfam; TIGR01003; PTS_HPr_family; 1.
DR   PANTHER; PTHR38594; PEP-DEPENDENT DIHYDROXYACETONE KINASE, PHOSPHORYL DONOR SUBUNIT DHAM; 1.
DR   PANTHER; PTHR38594:SF1; PEP-DEPENDENT DIHYDROXYACETONE KINASE, PHOSPHORYL DONOR SUBUNIT DHAM; 1.
DR   Pfam; PF03610; EIIA-man; 1.
DR   Pfam; PF00381; PTS-HPr; 1.
DR   PRINTS; PR00107; PHOSPHOCPHPR.
DR   SUPFAM; SSF55594; HPr-like; 1.
DR   SUPFAM; SSF53062; PTS system fructose IIA component-like; 1.
DR   PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
DR   PROSITE; PS51350; PTS_HPR_DOM; 1.
DR   PROSITE; PS00369; PTS_HPR_HIS; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000058305};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          3..141
FT                   /note="PTS EIIA type-4"
FT                   /evidence="ECO:0000259|PROSITE:PS51096"
FT   DOMAIN          148..231
FT                   /note="HPr"
FT                   /evidence="ECO:0000259|PROSITE:PS51350"
SQ   SEQUENCE   231 AA;  23050 MW;  2FC1BF793CFE3E48 CRC64;
     MARVGVVYVS HSEKITDGLL ELARQMAQNA PLAGAGGTDD GRIGTSFDKV SAGIAAVNQG
     VGVVVLCDLG SAILTAETAL DFLDDSVRET VRIVDAPLIE GGVAAAVASE VGASLLSVVE
     AAESASSTSP VAVAAAAEEP VAEQPGGGYT RTVTLVNKDG LHARPAADFV KLANTFGTKV
     TVNGTDARSL LGIMAMGLVK GTTVVLSTED PAGSDAVDAL AALIESGFGE I
//
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