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Database: UniProt
Entry: A0A1L7XXH9_9HELO
LinkDB: A0A1L7XXH9_9HELO
Original site: A0A1L7XXH9_9HELO 
ID   A0A1L7XXH9_9HELO        Unreviewed;       532 AA.
AC   A0A1L7XXH9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=DhaK domain-containing protein {ECO:0000259|PROSITE:PS51481};
GN   ORFNames=PAC_19654 {ECO:0000313|EMBL:CZR69754.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR69754.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR69754.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR69754.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-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; FJOG01000079; CZR69754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7XXH9; -.
DR   STRING; 576137.A0A1L7XXH9; -.
DR   OrthoDB; 6043at2759; -.
DR   UniPathway; UPA00617; UER00669.
DR   Proteomes; UP000184330; 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; 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.
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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184330};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..339
FT                   /note="DhaK"
FT                   /evidence="ECO:0000259|PROSITE:PS51481"
FT   REGION          401..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   532 AA;  56813 MW;  42EEEEBAC4061A45 CRC64;
     MSFGKHFIND VEDPVERGLK CLLRLNQSLR LIESERGGGL GHELAHAGYL DEGMLDICVV
     GQIVASPSAL QILAGLKALD TPRGILMIVK NYTGDKLNFG LAAQKATAQR IQVKVIFVGD
     DVSVKNNGLV GRRGLAGVAF VHKIAGALAA AGYVAEGSVQ PQSLTEYIQW HPGGATDIAQ
     RVADSISTAS VILDRCNVPR RGQQQSLPFE HLEYGMGIHN ESSVRRDTIP SFSTNITNIL
     SLLTPSAFNS TLPEAVMTNN LGSLSILEQN AIAGDLMDQL ERTGHDIRRM LVGTFATSLD
     GPGSSPATEK PCLPPVDTLL VQKITRSILE SVTRDEPLIT KYDTIAGDGD GGKTLLKGVN
     GKSLPSPSLP PSSILYTKLT HLPAPAIHDH FSRISSPHLD LITTSTQSPP QSKPAWAGPP
     ALSTQSSSTL SPTLFPQTQT LPWMSPPSSQ PPSNKHSQNS ATARQPVRGQ KTIMDALIPF
     IEAFAKTLDF ELAAREVERG SEGTRGLDAV LGRASYVSKE SLMEEESGMG VS
//
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