ID Q98C50_RHILO Unreviewed; 547 AA.
AC Q98C50;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Dihydroxyacetone kinase {ECO:0000313|EMBL:BAB51771.1};
GN OrderedLocusNames=mll5296 {ECO:0000313|EMBL:BAB51771.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB51771.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB51771.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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DR EMBL; BA000012; BAB51771.1; -; Genomic_DNA.
DR RefSeq; WP_010913110.1; NC_002678.2.
DR AlphaFoldDB; Q98C50; -.
DR KEGG; mlo:mll5296; -.
DR PATRIC; fig|266835.9.peg.4197; -.
DR eggNOG; COG2376; Bacteria.
DR HOGENOM; CLU_017054_6_2_5; -.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:InterPro.
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; IPR004006; DhaK_dom.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR PANTHER; PTHR28629; TRIOKINASE/FMN CYCLASE; 1.
DR PANTHER; PTHR28629:SF4; TRIOKINASE_FMN CYCLASE; 1.
DR Pfam; PF02733; Dak1; 1.
DR Pfam; PF02734; Dak2; 1.
DR SMART; SM01120; Dak2; 1.
DR SUPFAM; SSF82549; DAK1/DegV-like; 1.
DR SUPFAM; SSF101473; DhaL-like; 1.
DR PROSITE; PS51481; DHAK; 1.
DR PROSITE; PS51480; DHAL; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAB51771.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..325
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 355..542
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
SQ SEQUENCE 547 AA; 55556 MW; 29206251029ED4AE CRC64;
MKHFFNRRET IVTEALDGLL RTIGSGDLAR LDGYPEIKVV LRADWDKSRV SVVSGGGAGH
EPSHAGFVGK GMLTAAVSGE IFASPSVEAV LAAIRAVTGP AGCLLIVKNY TGDRLNFGLA
AEKARAEGFR VEMVIVADDI ALPDIAQPRG VAGTLFVHKI SGHLSEAGHN LADIAAAARA
AAKDIVSLGM SLSSCSIPGQ PHEDRFGADD GELGLGIHGE PGVERIALQS VDRLVAIMAE
RLAAGLDPKA SHALLINNLG AVPPLEMSLI ANAVLASPLA KTVKLTIGPG PLMTALNMNG
FSLSLIRLDA AREAALLAPV GPHAWMPAKP VAAPVIVPMA KAAGQSVAHK ASQDASSRRL
IVTVCEKLIS LEASLNGLDA KAGDGDTGST VATGARSILE RLDVLPLANP AATLGAIGDI
LSSSMGGSSG VLLSIFFTAA AQVLGGGASL SKALLAGLER MTFYGGAKPG DRTMVDALEP
ALKALDADGL EEAAAAAQRG AEATAAMEKA KAGRSAYVGT KLQGVVDPGA HAVAEVFSAA
ATLLVTA
//
