ID   MPDC_MYCAO              Reviewed;         504 AA.
AC   Q3YAT5;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Hydroxyisobutyraldehyde dehydrogenase {ECO:0000303|PubMed:16622053};
DE            EC=1.2.1.98 {ECO:0000269|PubMed:16622053};
GN   Name=mpdC {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], FUNCTION, CATALYTIC ACTIVITY,
RP   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 hydroxyisobutyraldehyde to
CC       hydroxyisobutyric acid (HIBA). {ECO:0000269|PubMed:16622053}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxy-2-methylpropanal + H2O + NAD(+) = 2-hydroxy-2-
CC         methylpropanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:49616,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:19641,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:131846;
CC         EC=1.2.1.98; Evidence={ECO:0000269|PubMed:16622053};
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 aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; DQ147773; AAZ78235.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3YAT5; -.
DR   SMR; Q3YAT5; -.
DR   KEGG; ag:AAZ78235; -.
DR   BioCyc; MetaCyc:MON-19854; -.
DR   BRENDA; 1.2.1.98; 14567.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN           1..504
FT                   /note="Hydroxyisobutyraldehyde dehydrogenase"
FT                   /id="PRO_0000447201"
FT   ACT_SITE        260
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P25526"
FT   ACT_SITE        294
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P25526"
SQ   SEQUENCE   504 AA;  53848 MW;  E3DFCF0822C37C09 CRC64;
     MTRTLSADAD TRTATPPLMY VNGEWLPARS GATFPTIEPS TGRPITEIPR GDSSDVDAAV
     KAAADVAVEW QFTDAITRAA LLRRLAELVA ENAEELARIE SLDSGHYLAK ARELVTAIPL
     WLEYWAGAAD KVGGRTIAVP GNKLSFTLLE PLGVTAHIIP WNYPLLILAR SIAPALALGN
     TCVVKPAEDT SLSALKFAEL VHAAGFPAGV FNVVTGYGSE AGAALAAHPE VRGITFTGST
     ETGREIARLG GQHIAQVNLE LGGKSPLVVF PDAPLEDAVE VAVQGFCSRA GQVCVAGSRL
     FLHEDIADRF LEMLVSRLET VTVGDPFDGA TQMGPLASKK HYDRVREYIE VGKQEATLLY
     GGGRPTDTPD DGFFVEPTVF VDVATDARIA REEIFGPVTA VMRWSSVDDL IATINDSEFG
     LFAVLWCRDI TSALDTAKRL QVGSVMINDW FGELPMTPHG GHKQSGTGRE EGLEAVHGYT
     QVKHIGINLE PSPAKSADWA GAPL