DAS_PICAN
ID DAS_PICAN Reviewed; 710 AA.
AC P06834;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Dihydroxyacetone synthase;
DE Short=DHAS;
DE EC=2.2.1.3;
DE AltName: Full=Formaldehyde transketolase;
DE AltName: Full=Glycerone synthase;
GN Name=DAS;
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC Y-5445;
RX PubMed=2987872; DOI=10.1093/nar/13.9.3043;
RA Janowicz Z.A., Eckart M.R., Drewke C., Roggenkamp R.O., Hollenberg C.P.,
RA Maat J., Ledeboer A.M., Visser C., Verrips C.T.;
RT "Cloning and characterization of the DAS gene encoding the major methanol
RT assimilatory enzyme from the methylotrophic yeast Hansenula polymorpha.";
RL Nucleic Acids Res. 13:3043-3062(1985).
RN [2]
RP SEQUENCE REVISION TO 509-510; 550-561 AND 586.
RA Veenhuis M.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 667-710, AND SEQUENCE REVISION.
RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC Y-5445;
RX PubMed=1465101; DOI=10.1007/bf00279370;
RA Hansen H., Didion T., Thiemann A., Veenhuis M., Roggenkamp R.O.;
RT "Targeting sequences of the two major peroxisomal proteins in the
RT methylotrophic yeast Hansenula polymorpha.";
RL Mol. Gen. Genet. 235:269-278(1992).
CC -!- FUNCTION: This is the major methanol assimilatory enzyme from the
CC methylotrophic Hansenula polymorpha.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-xylulose 5-phosphate + formaldehyde = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone; Xref=Rhea:RHEA:24264,
CC ChEBI:CHEBI:16016, ChEBI:CHEBI:16842, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:59776; EC=2.2.1.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+). {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; X02424; CAA26276.2; -; Genomic_DNA.
DR PIR; A23009; XJHQFK.
DR AlphaFoldDB; P06834; -.
DR SMR; P06834; -.
DR PhylomeDB; P06834; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0047896; F:formaldehyde transketolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; PTHR43522; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Methanol utilization; Peroxisome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..710
FT /note="Dihydroxyacetone synthase"
FT /id="PRO_0000191911"
FT MOTIF 708..710
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 433
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 128..130
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT SITE 38
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 275
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 710 AA; 78731 MW; E0E2A13BE9288357 CRC64;
MSMRIPKAAS VNDEQHQRII KYGRALVLDI VEQYGGGHPG SAMGAMAIGI ALWKYTLKYA
PNDPNYFNRD RFVLSNGHVC LFQYIFQHLY GLKSMTMAQL KSYHSNDFHS LCPGHPEIEH
DAVEVTTGPL GQGISNSVGL AIATKNLAAT YNKPGFDIIT NKVYCMVGDA CLQEGPALES
ISLAGHMGLD NLIVLYDNNQ VCCDGSVDIA NTEDISAKFK ACNWNVIEVE NASEDVATIV
KALEYAQAEK HRPTLINCRT VIGSGAAFEN HCAAHGNALG EDGVRELKIK YGMNPAQKFY
IPQDVYDFFK EKPAEGDKLV AEWKSLVAKY VKAYPEEGQE FLARMRGELP KNWKSFLPQQ
EFTGDAPTRA AARELVRALG QNCKSVIAGC ADLSVSVNLQ WPGVKYFMDP SLSTQCGLSG
DYSGRYIEYG IREHAMCAIA NGLAAYNKGT FLPITSTFFM FYLYAAPAIR MAGLQELKAI
HIGTHDSINE GENGPTHQPV ESPALFRAMP NIYYMRPVDS AEVFGLFQKA VELPFSSILS
LSRNEVLQYP GKSSAEKAQR GGYILEDAEN AEVQIIGVGA EMEFAYKAAK ILGRKFRTRV
LSIPCTRLFD EQSIGYRRSV LRKDGRQVPT VVVDGHVAFG WERYATASYC MNTYGKSLPP
EVIYEYFGYN PATIAKKVEA YVRACQRDPL LLHDFLDLKE KPNHDKVNKL
