MPDB_MYCAO
ID MPDB_MYCAO Reviewed; 552 AA.
AC Q3YAT3;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=2-methyl-1,2-propanediol dehydrogenase {ECO:0000305};
DE Short=2-M1,2-PD dehydrogenase {ECO:0000303|PubMed:16622053};
DE EC=1.1.1.400 {ECO:0000269|PubMed:16622053};
GN Name=mpdB {ECO:0000303|PubMed:16622053};
OS Mycolicibacterium austroafricanum (Mycobacterium austroafricanum).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=39687;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14; 58-73 AND
RP 111-140, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=IFP 2012;
RX PubMed=16622053; DOI=10.1099/mic.0.28585-0;
RA Lopes Ferreira N., Labbe D., Monot F., Fayolle-Guichard F., Greer C.W.;
RT "Genes involved in the methyl tert-butyl ether (MTBE) metabolic pathway of
RT Mycobacterium austroafricanum IFP 2012.";
RL Microbiology 152:1361-1374(2006).
CC -!- FUNCTION: Involved in the degradation of methyl tert-butyl ether
CC (MTBE). Catalyzes the conversion of 2-methyl 1,2-propanediol (2-M1,2-
CC PD) to hydroxyisobutyraldehyde. {ECO:0000269|PubMed:16622053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpropane-1,2-diol + NAD(+) = 2-hydroxy-2-methylpropanal
CC + H(+) + NADH; Xref=Rhea:RHEA:23552, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:131845,
CC ChEBI:CHEBI:131846; EC=1.1.1.400;
CC Evidence={ECO:0000269|PubMed:16622053};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:M1VMF7};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16622053}.
CC -!- INDUCTION: Induced in the presence of MTBE or tert-butyl alcohol (TBA).
CC {ECO:0000269|PubMed:16622053}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; DQ147773; AAZ78237.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YAT3; -.
DR SMR; Q3YAT3; -.
DR KEGG; ag:AAZ78237; -.
DR BioCyc; MetaCyc:MON-19853; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..552
FT /note="2-methyl-1,2-propanediol dehydrogenase"
FT /id="PRO_0000447200"
FT CONFLICT 111
FT /note="G -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 60181 MW; 8268ACD81410C31F CRC64;
MTTSADQTDV LVIGSGPGGA GVTLKLVQAG YKVTCLEQGP WVTPPEHPHY HREWEIEKQR
GWAYDPNVRG LPEDYPVTGF TTPYLMNNVG GSTMHYAGHW PRYKPVDFRK GTEHGLEGTI
DWPISYEELA PYYDENDAIY GISGMVGDPS YPDRTGVDRD PPVKPGKLGR NFAQALGDLG
WHWWPSDNAI ITRPREGREA DIAAGNELSG SPTGSLSTPT HTHWPTAIAL GADLRTHARV
EQIHTKNGKA TGATYIDTRT GARHEINAKI VVVSASGIGT PRLLLMSAQK GHPDGLANSN
GLVGKYLMHH ILRVLASVVR TSRMEGYKGA FGAPLYSHEF YHTDTNRGFV NGFGMQVARS
FGAAYTAMGS HTGYVAPWGK SHRKFFNEHF GNHLMVFMFG EDLPVETNCV TLDPDAKDSS
GLPAARVNWE PHENDIALAN YGIDRIFEAA RALGAVETND TGVLNPPPGW HLMGTCRMGN
NPEDSVTNKW HQTWDVPNLF VVDGSSLTTG GAVNPTSTIG ALAVRAGDYI SRRFSDIVDQ
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