DAS_CANBO
ID DAS_CANBO Reviewed; 706 AA.
AC O93884;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 83.
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=DAS1;
OS Candida boidinii (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX NCBI_TaxID=5477;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-22.
RC STRAIN=S2;
RX PubMed=9811645; DOI=10.1128/jb.180.22.5885-5890.1998;
RA Sakai Y., Nakagawa T., Shimase M., Kato N.;
RT "Regulation and physiological role of the DAS1 gene, encoding
RT dihydroxyacetone synthase, in the methylotrophic yeast Candida boidinii.";
RL J. Bacteriol. 180:5885-5890(1998).
CC -!- FUNCTION: Involved in assimilation of formaldehyde.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; AF086822; AAC83349.1; -; Genomic_DNA.
DR AlphaFoldDB; O93884; -.
DR SMR; O93884; -.
DR BioCyc; MetaCyc:MON-13164; -.
DR BRENDA; 2.2.1.3; 1100.
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 1: Evidence at protein level;
KW Direct protein sequencing; Magnesium; Metal-binding; Methanol utilization;
KW Peroxisome; Thiamine pyrophosphate; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9811645"
FT CHAIN 2..706
FT /note="Dihydroxyacetone synthase"
FT /id="PRO_0000191910"
FT MOTIF 704..706
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 431
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 126..128
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 459
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT SITE 36
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 273
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 706 AA; 78137 MW; 9DC3B993B972DE81 CRC64;
MALAKAASIN DDIHDLTMRA FRCYVLDLVE QYEGGHPGSA MGMVAMGIAL WKYTMKYSTN
DPTWFNRDRF VLSNGHVCLF QYLFQHLSGL KSMTEKQLKS YHSSDYHSKC PGHPEIENEA
VEVTTGPLGQ GISNSVGLAI ASKNLGALYN KPGYEVVNNT TYCIVGDACL QEGPALESIS
FAGHLGLDNL VVIYDNNQVC CDGSVDIANT EDISAKFRAC NWNVIEVEDG ARDVATIVKA
LELAGAEKNR PTLINVRTII GTDSAFQNHC AAHGSALGEE GIRELKIKYG FNPSQKFHFP
QEVYDFFSDI PAKGDEYVSN WNKLVSSYVK EFPELGAEFQ SRVKGELPKN WKSLLPNNLP
NEDTATRTSA RAMVRALAKD VPNVIAGSAD LSVSVNLPWP GSKYFENPQL ATQCGLAGDY
SGRYVEFGIR EHCMCAIANG LAAFNKGTFL PITSSFYMFY LYAAPALRMA ALQELKAIHI
ATHDSIGAGE DGPTHQPIAQ SALWRAMPNF YYMRPGDASE VRGLFEKAVE LPLSTLFSLS
RHEVPQYPGK SSIELAKRGG YVFEDAKDAD IQLIGAGSEL EQAVKTARIL RSRGLKVRIL
SFPCQRLFDE QSVGYRRSVL QRGKVPTVVI EAYVAYGWER YATAGYTMNT FGKSLPVEDV
YEYFGFNPSE ISKKIEGYVR AVKANPDLLY EFIDLTEKPK HDQNHL
