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Database: UniProt
Entry: E6R1Q6_CRYGW
LinkDB: E6R1Q6_CRYGW
Original site: E6R1Q6_CRYGW 
ID   E6R1Q6_CRYGW            Unreviewed;       591 AA.
AC   E6R1Q6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-NOV-2023, entry version 53.
DE   SubName: Full=Dihydroxyacetone kinase 1, putative {ECO:0000313|EMBL:ADV21190.1};
GN   OrderedLocusNames=CGB_C6280C {ECO:0000313|EMBL:ADV21190.1};
OS   Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS   (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=367775 {ECO:0000313|EMBL:ADV21190.1, ECO:0000313|Proteomes:UP000007805};
RN   [1] {ECO:0000313|EMBL:ADV21190.1, ECO:0000313|Proteomes:UP000007805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM276 / ATCC MYA-4071 {ECO:0000313|Proteomes:UP000007805};
RX   PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA   McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA   Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA   Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA   Fyfe M., Ouellette B.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA   Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 2:E342-E342(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WM276;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA   McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA   Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA   Schein J., Krzywinski M., Kwong-Chung K.J., Varma A., Wang J., Brunham R.,
RA   Fyfe M., Ouellette B.F.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA   Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 0:0-0(2011).
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; CP000288; ADV21190.1; -; Genomic_DNA.
DR   RefSeq; XP_003192977.1; XM_003192929.1.
DR   AlphaFoldDB; E6R1Q6; -.
DR   GeneID; 10187730; -.
DR   KEGG; cgi:CGB_C6280C; -.
DR   VEuPathDB; FungiDB:CGB_C6280C; -.
DR   eggNOG; KOG2426; Eukaryota.
DR   HOGENOM; CLU_017054_6_0_1; -.
DR   OrthoDB; 6043at2759; -.
DR   UniPathway; UPA00617; UER00669.
DR   Proteomes; UP000007805; Chromosome C.
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; 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   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:ADV21190.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          11..352
FT                   /note="DhaK"
FT                   /evidence="ECO:0000259|PROSITE:PS51481"
FT   DOMAIN          387..588
FT                   /note="DhaL"
FT                   /evidence="ECO:0000259|PROSITE:PS51480"
FT   ACT_SITE        223
FT                   /note="Tele-hemiaminal-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT   BINDING         55..58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ   SEQUENCE   591 AA;  62161 MW;  D3CFD6ECAAF3171C CRC64;
     MAPAQKHLLN TPHTLVVDSL KGLATLNPNV KLDEAQRVIY TPPSESKVAL LSGGGSGHEP
     AHAAFVGPGL LSAAICGNIF ASPNVAQIRR GLELVTREKG SLIVVMNYTG DALHFGLAAE
     QHRSAGKVGD VRVLMVGDDV AVGRQQGSIV GRRGLAGTIL VYKVAAALSD KGADLDSVEN
     IAKYVASRLG TLGVGLEHCH VPGTRAGTSH LGANEVEVGM GIHNEAGTYK LDMTTVSELV
     GRMLTQITDT TDKDKSFVPF KGDGSDEVVL LVNDLGAISE LEMGGITNEA VKWLQSRNIK
     VRRVLAGTYM TSLNMPGFSL TLLLLPSASE KPPHSAHEIL EYLDAPASAP GWKWHAGREP
     GTLDVKTEEA SIPVQKDNAV LPSTDSKGFL AAITRACKAL IAAEPELTEQ DQIAGDGDAG
     LTLEAGAKGV LKAIEQGRLK GENVVQDIKI IAEIVEEDMG GTSGALYSIF FAGLGKSLRD
     AATNGAKNTT PEVWSKAAAG ALDTLYKYTR ARPPSRTLVD PLDAFIASLP SKGLSSAAED
     ALAAADKTKE LVAKAGRGAY VNQEDLKKRE VPDPGAWGIW RIVDGLRGFE A
//
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