ID R0INB5_9BRAS Unreviewed; 524 AA.
AC R0INB5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=3,4-dihydroxy-2-butanone kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CARUB_v10008842mg {ECO:0000313|EMBL:EOA40135.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA40135.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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DR EMBL; KB870805; EOA40135.1; -; Genomic_DNA.
DR RefSeq; XP_006307237.1; XM_006307175.1.
DR AlphaFoldDB; R0INB5; -.
DR STRING; 81985.R0INB5; -.
DR eggNOG; KOG2426; Eukaryota.
DR Proteomes; UP000029121; Unassembled WGS sequence.
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; IPR012734; DhaK_ATP.
DR InterPro; IPR004006; DhaK_dom.
DR InterPro; IPR004007; DhaL_dom.
DR InterPro; IPR036117; DhaL_dom_sf.
DR NCBIfam; TIGR02361; dak_ATP; 1.
DR PANTHER; PTHR28629:SF13; DIHYDROXYACETONE KINASE; 1.
DR PANTHER; PTHR28629; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..265
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 304..508
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT REGION 263..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 524 AA; 53965 MW; B2FE8C83D36981DC CRC64;
MLTAAICGDV FTSPPVDSIL AGIRAVTGPK GCLLVVTNYT GDRLNFGLAA EQAKTEGFQI
ETVIVGDDCA LPPPRGIAGR RGLAGTILVH KVAGAAAAAG LSLAEVAAEA KHASEMVGTM
GVALSACALP GQVTSDRLGP EKMELGLGVH GEPGAAVVDI QPVEVVVSHV LQQILSPETN
YVPITRGNSV VLMVNGLGGT PLMELLIAAG KAVPKLQLEF GLAVDRVYTG SFMTSLDMAG
FSISIMKADQ SILERLDAPT KAPSWPVGTA GNRPPAKIPV PLPSQATKSE ESLSRPQALS
QQGKILEAAI EAAATVVINL KDSLNEWDGK VGDGDCGSTM CRGATAILED MKNYYPLNDA
AETVSEIGSS IRRVMGGTSG IIYNLLCKAA YAELKANGQP ETTPKHWSEA LKSSISAVSK
YGGATAGYRT MLDALIPASK ILEEKLSAGE DPITAFILSA EAATAGAEST IHMQAQAGRS
SYVSAEILAS IPDPGAMAVA AWYSAAARAV KEKSQGLGSD GLLC
//
