ID J4KNN2_BEAB2 Unreviewed; 599 AA.
AC J4KNN2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Dihydroxyacetone kinase {ECO:0000313|EMBL:EJP65999.1};
GN ORFNames=BBA_04970 {ECO:0000313|EMBL:EJP65999.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP65999.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP65999.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP65999.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
CC -!- FUNCTION: Catalyzes both the phosphorylation of dihydroxyacetone and of
CC glyceraldehyde. {ECO:0000256|ARBA:ARBA00003264}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate +
CC H(+); Xref=Rhea:RHEA:13941, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:59776, ChEBI:CHEBI:456216;
CC EC=2.7.1.28; Evidence={ECO:0000256|ARBA:ARBA00000031};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate +
CC H(+); Xref=Rhea:RHEA:15773, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57642, ChEBI:CHEBI:456216;
CC EC=2.7.1.29; Evidence={ECO:0000256|ARBA:ARBA00001015};
CC -!- PATHWAY: Polyol metabolism; glycerol fermentation; glycerone phosphate
CC from glycerol (oxidative route): step 2/2.
CC {ECO:0000256|ARBA:ARBA00004778}.
CC -!- SIMILARITY: Belongs to the dihydroxyacetone kinase (DAK) family.
CC {ECO:0000256|ARBA:ARBA00008757}.
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DR EMBL; JH725161; EJP65999.1; -; Genomic_DNA.
DR RefSeq; XP_008598289.1; XM_008600067.1.
DR AlphaFoldDB; J4KNN2; -.
DR STRING; 655819.J4KNN2; -.
DR GeneID; 19887982; -.
DR HOGENOM; CLU_017054_6_0_1; -.
DR InParanoid; J4KNN2; -.
DR OrthoDB; 6043at2759; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004371; F:glycerone kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0050354; F:triokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019588; P:anaerobic glycerol catabolic process; IEA:UniProtKB-UniPathway.
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:SF14; CHROMOSOME 1, WHOLE GENOME SHOTGUN SEQUENCE; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EJP65999.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..351
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 385..593
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT REGION 357..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 218
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT BINDING 54..57
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 599 AA; 62981 MW; 7A366FE710CFADAD CRC64;
MSKRHLFDSS DGLVNKALRG IIRYNPSLSL DEANRVVFDS DYDKSKVVLI SGGGSGHEPG
WSGYVGQNML TAAVQGDIFA SPSTKQIVAG VDAVPSDKGT ILVITNYTGD CLHFGLANEK
ATAKGHRCRT IICGDDVSVG RKGSLVGRRG LAGQIGVLKV MGGAAGAGAS LDEVYDLGVA
FSQQIVSIAA TLDHCHVPGR AEHATLKDDE VELGTGPHNE PGYKKLSPAP TPQDLVKQIL
THCLDEKDPE RGYVHFSPGD ETMLLVSNFG GMSHLEMGAL VDELLEQLER DWRMDPTRVC
AGFLETSLNA PAFSVSVINI TAAARNCSYS ADQIKAFFDA RTNTYWESVA GAQSKRRARK
DQLVSAPEPE HKTADDARDL KTDPALLETM LRTACDDLVK AEPDLTKWDT VMGDGDCGET
LKTGATALLA ALDAGLAKKG SVVSVLLELE DIVESKMGGT LGGILGIFFV SLRAAVEKNI
ALAQSADGGG AVALWGVALA TALENLRRYT PAQVGDRTVI DTLMPFADAM GKAGFDAAVD
AAVKGAEATK TMTPRLGRAT YVGGGGGGSG ANQEMPPDPG AWGAMVVIAG LYKAFNGKQ
//
