ID A0A094AE33_9PEZI Unreviewed; 1121 AA.
AC A0A094AE33;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DhaK domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V491_00791 {ECO:0000313|EMBL:KFY27674.1};
OS Pseudogymnoascus sp. VKM F-3775.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY27674.1, ECO:0000313|Proteomes:UP000029338};
RN [1] {ECO:0000313|EMBL:KFY27674.1, ECO:0000313|Proteomes:UP000029338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY27674.1,
RC ECO:0000313|Proteomes:UP000029338};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY27674.1}.
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DR EMBL; JPJT01000397; KFY27674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094AE33; -.
DR HOGENOM; CLU_290046_0_0_1; -.
DR UniPathway; UPA00617; UER00669.
DR Proteomes; UP000029338; 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 InterPro; IPR021858; Fun_TF.
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 Pfam; PF11951; Fungal_trans_2; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000029338};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..303
FT /note="DhaK"
FT /evidence="ECO:0000259|PROSITE:PS51481"
FT DOMAIN 337..548
FT /note="DhaL"
FT /evidence="ECO:0000259|PROSITE:PS51480"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 185
FT /note="Tele-hemiaminal-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-1"
FT BINDING 17..20
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612734-2"
SQ SEQUENCE 1121 AA; 122332 MW; 8034F2BBC3BCAD14 CRC64;
MARFSPDLAL DSTDKRGSGH EPAHAGYVGE GMLDVAVVGN IFASPSAAQV FKAIRAFPSE
QGTLIITKNY TGDVLSFGLA AEKAKAAGLK CKLLVVGDDI SIPCKEGSIV GRRGLAGTAL
VQKIAGAAAA EGNNLQEVYE IAKSVADNLA TIGVSLDRCH VPGRTTNLEN DTMGNAELEY
GMGIHNEPGV QRSCLKSLEE TVRQLLSRLF DENESGHTFI TWNKNDDIAL SLNNLGGLSV
LELHAILDET MDQLSRKYCI TPRRVLRGTM VSSFNGLGFS ITLLKLSDKM IPLLDRSTSA
PGWVPAAQFD NELESCEIKL SSPDTSFPLA RMKVEPCVFH KVLDEISKGI GADEPAITYF
DTITGDGDCG ETLLAGSNAI TAALQSGQIN TSDLISGLHT ISSVVEHSMG GTSGAIYSIY
LNALVSALSK IASTSSSSEV NSLDLAAAGA QALNELFKYT QARVGSRTMM DVLIPFIEHL
AARPGRLENA LAAAIKGAEA TKKMEASFGR ASYVDKAIFS KVDEGSGDAG IPDAGALGVL
SIFRAIFHVN WGSLLEQQRR AELGSEVATM FTTPFDDESS AKKRPNSRSR QGCLTCRRRR
LKWTNVHRPL AWKFVDNTEE IENGYYNYGL SPDNLDDRDD NGADLANAAT LNKNDVLIDP
VMAHRSKDTP DAPSLAGGLC LETSDQIFVS SDQQAAYSPT SSRNQPHEQD RRMRVNLISG
VESDISGNFQ ASQTFSPSEI ATPSPSSLNN GDNLPPWPID DKKKAMLIAS YLRETATWCE
TTDSMRHFSL QTSQDLLTSQ AHSAASVAVA SRQQDNLMGD ARLETLELYD FARETICSLE
TWQNDKLVLA GALQLCVYCM MSMEVNEWRL HLRGCAGTFQ EMGWNGSSGG LPAACFWAFA
RIDIWAAYLT QQRTLIPTDF WISSNYDEEG IDPLQDRYAN KAIWIFGRLI NELSELGQTA
RENSRSYGPY LHEFWQLWNE LDAWKAERPA SMKSLIELEP SKGDVFPFIL YGNFSASKIT
MPRERCCILL LEAGLKPPSN ADNSPEFSPL WHARRIGGIS LATDSHANWV NNLQPLFIAA
RHYTEAGEMI AILKHLKDIE VTTGWKTSSR STELRALWGL G
//
