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Database: UniProt
Entry: S9SCC0_9RHOB
LinkDB: S9SCC0_9RHOB
Original site: S9SCC0_9RHOB 
ID   S9SCC0_9RHOB            Unreviewed;       204 AA.
AC   S9SCC0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Dihydroxyacetone kinase DhaL subunit {ECO:0000313|EMBL:EPX87770.1};
DE            EC=2.7.1.- {ECO:0000313|EMBL:EPX87770.1};
DE            EC=2.7.1.121 {ECO:0000313|EMBL:EPX87770.1};
GN   ORFNames=ruthe_00173 {ECO:0000313|EMBL:EPX87770.1};
OS   Rubellimicrobium thermophilum DSM 16684.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX87770.1, ECO:0000313|Proteomes:UP000015346};
RN   [1] {ECO:0000313|EMBL:EPX87770.1, ECO:0000313|Proteomes:UP000015346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX87770.1,
RC   ECO:0000313|Proteomes:UP000015346};
RX   PubMed=24501632; DOI=10.4056/sigs.4247911;
RA   Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT   "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT   type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL   Stand. Genomic Sci. 8:480-490(2013).
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:EPX87770.1}.
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DR   EMBL; AOLV01000002; EPX87770.1; -; Genomic_DNA.
DR   RefSeq; WP_021096315.1; NZ_KE557318.1.
DR   AlphaFoldDB; S9SCC0; -.
DR   STRING; 1123069.ruthe_00173; -.
DR   PATRIC; fig|1123069.3.peg.179; -.
DR   HOGENOM; CLU_066424_2_0_5; -.
DR   OrthoDB; 9800291at2; -.
DR   Proteomes; UP000015346; Unassembled WGS sequence.
DR   GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
DR   GO; GO:0047324; F:phosphoenolpyruvate-glycerone phosphotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.340; -; 1.
DR   InterPro; IPR012737; DhaK_L_YcgS.
DR   InterPro; IPR004007; DhaL_dom.
DR   InterPro; IPR036117; DhaL_dom_sf.
DR   NCBIfam; TIGR02365; dha_L_ycgS; 1.
DR   PANTHER; PTHR28629; TRIOKINASE/FMN CYCLASE; 1.
DR   PANTHER; PTHR28629:SF4; TRIOKINASE_FMN CYCLASE; 1.
DR   Pfam; PF02734; Dak2; 1.
DR   SMART; SM01120; Dak2; 1.
DR   SUPFAM; SSF101473; DhaL-like; 1.
DR   PROSITE; PS51480; DHAL; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EPX87770.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015346};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPX87770.1}.
FT   DOMAIN          5..196
FT                   /note="DhaL"
FT                   /evidence="ECO:0000259|PROSITE:PS51480"
SQ   SEQUENCE   204 AA;  20691 MW;  061177C40CDCCF07 CRC64;
     MFTTDDLKTL FAAFAARMAT ERDHLCALDG AIGDGDHGIA MEQGMAAAAK AAAETEGTLQ
     DICNAAAKGF LNAVGASSGP LYATGFLRAG KALGPVTSVP QAQVLSIIPA IRDGIAHRGK
     AVPGQKTMLD TWHPAAEAVI GGATAAEVLR TATEGAEATR AMTATLGRAE RLGARAVGHP
     DPGAVSALML IEEILARIVP PPAD
//
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