ID   THCA_RHOER              Reviewed;         506 AA.
AC   P46369;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=EPTC-inducible aldehyde dehydrogenase;
DE            EC=1.2.1.3;
GN   Name=thcA;
OS   Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=1833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=NI86/21;
RX   PubMed=7836301; DOI=10.1128/jb.177.3.676-687.1995;
RA   Nagy I., Schoofs G., Compernolle F., Proost P., Vanderleyden J., de Mot R.;
RT   "Degradation of the thiocarbamate herbicide EPTC (S-ethyl
RT   dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21
RT   involve an inducible cytochrome P-450 system and aldehyde dehydrogenase.";
RL   J. Bacteriol. 177:676-687(1995).
CC   -!- FUNCTION: Degrades all aldehydes potentially generated by N
CC       dealkylation of thiocarbamates and may also participate in ethanolamine
CC       metabolism and further assimilation of degradation products by
CC       thiocarbamate-induced cytochrome P-450.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC   -!- INDUCTION: By EPTC (S-ethyl dipropylcarbamothioate).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U17129; AAC77472.1; -; Genomic_DNA.
DR   AlphaFoldDB; P46369; -.
DR   SMR; P46369; -.
DR   STRING; 1833.XU06_08920; -.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
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; IPR016160; Ald_DH_CS_CYS.
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; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..506
FT                   /note="EPTC-inducible aldehyde dehydrogenase"
FT                   /id="PRO_0000056453"
FT   ACT_SITE        263
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000250"
FT   BINDING         219..225
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   506 AA;  54994 MW;  DDA25B7138B34B37 CRC64;
     MTKYARPGTA DAIMSFQSRY DNWIGNEWVA PVKGQYFENP TPVTGQNFCD VARSTAEDIE
     LALDAAHAAA PAWGKTSVAE RAIILNKIAD RMEENLESIA LAESWDNGKP IRETLNADIP
     LAIDHFRYFA GAIRAQEGSL SEINSDTVAY HFHEPLGVVG QIIPWNFPIL MAVWKLAPAL
     AAGNAIVLKP AEQTPVSILH LIGIIGDLLP AGVLNIVNGF GVEAGKPLAS SPRIKKIAFT
     GETTTGRLIM QYASQNLIPV TLELGGKSPN VFFSDVLASN DDYQDKALEG FTMFALNQGE
     VCTAPSRALI QEDIFDEFLA MAAIRTKAVR QGDPLDTDTM IGAQASNDQL EKILSYIEIG
     KAEGAKVITG GERAELGGDL SGGYYVQPTV FTGNNKMRIF QEIFGPVVSV TSFKDYDEAI
     EIANDTLYGL GAGVWSRDGG VAYRAGRDIQ AGRVWTNTYH QYPAHAAFGG YKQSGIGREN
     HLMMLSHYQQ TKNLLVSYAQ KAQGFF