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Database: UniProt
Entry: A0A178E8R6_9PLEO
LinkDB: A0A178E8R6_9PLEO
Original site: A0A178E8R6_9PLEO 
ID   A0A178E8R6_9PLEO        Unreviewed;       567 AA.
AC   A0A178E8R6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   08-NOV-2023, entry version 18.
DE   SubName: Full=Dihydroxyacetone kinase {ECO:0000313|EMBL:OAL51699.1};
GN   ORFNames=IQ07DRAFT_610501 {ECO:0000313|EMBL:OAL51699.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL51699.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL51699.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL51699.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV441642; OAL51699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178E8R6; -.
DR   STRING; 765867.A0A178E8R6; -.
DR   InParanoid; A0A178E8R6; -.
DR   OrthoDB; 6043at2759; -.
DR   UniPathway; UPA00617; UER00669.
DR   Proteomes; UP000077535; 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; 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:OAL51699.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          8..326
FT                   /note="DhaK"
FT                   /evidence="ECO:0000259|PROSITE:PS51481"
FT   DOMAIN          367..563
FT                   /note="DhaL"
FT                   /evidence="ECO:0000259|PROSITE:PS51480"
FT   ACT_SITE        220
FT                   /note="Tele-hemiaminal-histidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT   BINDING         53..56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ   SEQUENCE   567 AA;  60497 MW;  FE75698F4DCCA384 CRC64;
     MVTTFYDDSE TPVLEALEAL EFLQPGISFD QDQKTVWRSK YDQQHVSLLS GGGAGHEPAH
     AGFVGVGMLT AAVSGWIFAS PSVNQIVSGI ARVQSKSGVL LIIKNYTGDM FYFHLAAEKA
     SVKFGIPVEV LVVGDDVAVG RRKSGKVGRR GLAGTVLVHK ILGARSLELD ASLASLLALG
     RQVTENLVTV GASLEHVQVP GRAQSTTTRD DHVELGMGIH NETGSQILSP RPRLPHLIKM
     MLDQLLNQDD GDRSYVDFSN AEEIVLLVNN LGGISKLEIG GITLKSRVLS GTYMTSLNGL
     GFSISLLKAT PIMLRYIDAP TDARDWIKAT MPQWDAKERQ PAIQQCSNEV EGNISLPGFN
     DTLGDDKILK AAVKMACKNL LEAEPVITDY DNQVGDGDCG ITLARGATAV QARIDLSDDN
     TGAIQTILRI AEAIESNMDG TSGAVYGIFF TALAAALQSS GKGSTTAEQW SAAAKTALTK
     LQQATPARQG DRTVMDALEP FILAISEGCD LDKAVSLARE GMEATKGMRP AFGRAVYVEE
     KAWSLVPDPG AKGVLCIIEG IRDSISL
//
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