ID   BOXD_AROEV              Reviewed;         515 AA.
AC   Q84HH8;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
DE            EC=1.2.1.77;
GN   Name=boxD;
OS   Aromatoleum evansii (Azoarcus evansii).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=59406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX   PubMed=12399500; DOI=10.1128/jb.184.22.6301-6315.2002;
RA   Gescher J., Zaar A., Mohamed M.E.-S., Schaegger H., Fuchs G.;
RT   "Genes coding for a new pathway of aerobic benzoate metabolism in Azoarcus
RT   evansii.";
RL   J. Bacteriol. 184:6301-6315(2002).
RN   [2]
RP   CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX   PubMed=16585753; DOI=10.1128/jb.188.8.2919-2927.2006;
RA   Gescher J., Ismail W., Oelgeschlaeger E., Eisenreich W., Woerth J.,
RA   Fuchs G.;
RT   "Aerobic benzoyl-coenzyme A (CoA) catabolic pathway in Azoarcus evansii:
RT   conversion of ring cleavage product by 3,4-dehydroadipyl-CoA semialdehyde
RT   dehydrogenase.";
RL   J. Bacteriol. 188:2919-2927(2006).
CC   -!- FUNCTION: Catalyzes the NADP-dependent oxidation of 3,4-dehydroadipyl-
CC       CoA semialdehyde to form cis-3,4-dehydroadipyl-CoA.
CC       {ECO:0000269|PubMed:16585753}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3Z)-6-oxohex-3-enoyl-CoA + H2O + NADP(+) = cis-3,4-
CC         dehydroadipyl-CoA + 2 H(+) + NADPH; Xref=Rhea:RHEA:25391,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:58786, ChEBI:CHEBI:58787; EC=1.2.1.77;
CC         Evidence={ECO:0000269|PubMed:16585753};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=25 uM for 3,4-dehydroadipyl-CoA semialdehyde
CC         {ECO:0000269|PubMed:16585753};
CC         KM=16 uM for NADP {ECO:0000269|PubMed:16585753};
CC         Vmax=7.5 umol/min/mg enzyme for the forward reaction
CC         {ECO:0000269|PubMed:16585753};
CC       pH dependence:
CC         Optimum pH is 7.2. {ECO:0000269|PubMed:16585753};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16585753}.
CC   -!- INDUCTION: By benzoate. {ECO:0000269|PubMed:12399500}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AF548005; AAN39373.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q84HH8; -.
DR   SMR; Q84HH8; -.
DR   KEGG; ag:AAN39373; -.
DR   BioCyc; MetaCyc:MON-15415; -.
DR   SABIO-RK; Q84HH8; -.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
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; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; NADP; Oxidoreductase.
FT   CHAIN           1..515
FT                   /note="3,4-dehydroadipyl-CoA semialdehyde dehydrogenase"
FT                   /id="PRO_0000350729"
FT   REGION          470..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   515 AA;  53598 MW;  6E46066FCBF1FADC CRC64;
     MKLANYVYGQ WIEGAGEGAA LTDPVTGEAL VRVSSDGIDV ARALEFARTA GGAALKALTY
     EERAAKLAAI AELLQAKRAE YFDISLRNSG ATEGDASFDV DGAIFTVKSY ARAGKALGAG
     RHLKEGGRVA LAKTDVFQGQ HFLMPLTGVA VFINAFNFPA WGLWEKAAPA LLAGVPVFAK
     PATPTAWLAQ RMVADVVEAG ILPPGAISIV CGGARDLLDH VTECDVVSFT GSADTAARMR
     THPNVVARSV RINIEADSVN SAILGPDAQP GTPEFDLAVK EIVREMTVKT GQKCTAIRRI
     LAPAGVSRAL ADAVSGKLAG CKVGNPRSEG VRVGPLVSKA QQAAAFEGLA KLRQECEVVF
     GGDPDFEPVD ADAAVSAFVQ PTLLYCDKGL AARHVHDVEV FGPVATMVPY ADTRDAVAIA
     RRGHGSLVAS VYSGDAAFLG ELVPGIADLH GRVMVVDAAV GANHTGHGNV MPTCLHGGPR
     ARRRRRGVGR SARAGDVSPP LRRAGRPRGA GSPVA