ID   PCHA_PSEPU              Reviewed;         491 AA.
AC   Q59702;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=4-hydroxybenzaldehyde dehydrogenase (NADP(+)) {ECO:0000303|PubMed:23736872};
DE            Short=PHBDD {ECO:0000303|PubMed:23736872};
DE            EC=1.2.1.96 {ECO:0000269|PubMed:23736872};
GN   Name=pchA;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OG   Plasmid pRA4000.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCIMB 9866; PLASMID=pRA4000;
RX   PubMed=7929007; DOI=10.1128/jb.176.20.6349-6361.1994;
RA   Kim J.-H., Fuller J.H., Cecchini G., McIntire W.S.;
RT   "Cloning, sequencing, and expression of the structural genes for the
RT   cytochrome and flavoprotein subunits of p-cresol methylhydroxylase from two
RT   strains of Pseudomonas putida.";
RL   J. Bacteriol. 176:6349-6361(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCIMB 9866; PLASMID=pRA4000;
RX   PubMed=10565539; DOI=10.3109/10425179909033930;
RA   Cronin C.N., Kim J.-H., Fuller J.H., Zhang X.-P., McIntire W.S.;
RT   "Organization and sequences of p-hydroxybenzaldehyde dehydrogenase and
RT   other plasmid-encoded genes for early enzymes of the p-cresol degradative
RT   pathway in Pseudomonas putida NCIMB 9866 and 9869.";
RL   DNA Seq. 10:7-17(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, AND SUBSTRATE
RP   SPECIFICITY.
RC   STRAIN=NCIMB 9866; PLASMID=pRA4000;
RX   PubMed=23736872; DOI=10.1007/s00253-013-5001-z;
RA   Chen Y.F., Chao H., Zhou N.Y.;
RT   "The catabolism of 2,4-xylenol and p-cresol share the enzymes for the
RT   oxidation of para-methyl group in Pseudomonas putida NCIMB 9866.";
RL   Appl. Microbiol. Biotechnol. 98:1349-1356(2014).
CC   -!- FUNCTION: Involved in p-cresol and 2,4-xylenol catabolism. Catalyzes
CC       the oxidation of 4-hydroxybenzaldehyde and 4-hydroxy-3-
CC       methylbenzaldehyde to yield 4-hydroxybenzoic acid and 4-hydroxy-3-
CC       methylbenzoic acid, respectively. {ECO:0000269|PubMed:23736872}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxybenzaldehyde + H2O + NADP(+) = 4-hydroxybenzoate + 2
CC         H(+) + NADPH; Xref=Rhea:RHEA:47936, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17597, ChEBI:CHEBI:17879,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.96;
CC         Evidence={ECO:0000269|PubMed:23736872};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.57 uM for 4-hydroxybenzaldehyde (with NADP)
CC         {ECO:0000269|PubMed:23736872};
CC         KM=6.36 uM for 4-hydroxy-3-methylbenzaldehyde (with NADP)
CC         {ECO:0000269|PubMed:23736872};
CC         KM=20.55 uM for 4-hydroxy-3-methylbenzaldehyde (with NAD)
CC         {ECO:0000269|PubMed:23736872};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are still able to produce
CC       4-hydroxy-3-methylbenzoic acid and 4-hydroxybenzoic acid.
CC       {ECO:0000269|PubMed:23736872}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U96338; AAA75634.2; -; Genomic_DNA.
DR   EMBL; KC762703; AGO01127.1; -; Genomic_DNA.
DR   PIR; T46684; T46684.
DR   AlphaFoldDB; Q59702; -.
DR   SMR; Q59702; -.
DR   KEGG; ag:AGO01127; -.
DR   BioCyc; MetaCyc:MON-19470; -.
DR   BRENDA; 1.2.1.96; 5092.
DR   SABIO-RK; Q59702; -.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR   GO; GO:1901785; P:p-cresol catabolic process; IDA:UniProtKB.
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   NAD; NADP; Oxidoreductase; Plasmid.
FT   CHAIN           1..491
FT                   /note="4-hydroxybenzaldehyde dehydrogenase (NADP(+))"
FT                   /id="PRO_0000435508"
FT   ACT_SITE        259
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
SQ   SEQUENCE   491 AA;  53156 MW;  70C45CE421266344 CRC64;
     MSQRLAAYEN MSLQLIAGEW RVGKAGRDLD VLDPFTQEKL LQIPLANRED LDEAYRSARQ
     AQVAWAACGP SERAQVMLNA VRIFDERRDE IIDWIIRESG STRIKAQIEW GAARAITQES
     ASLPSRVHGR ILASDVPGKE SRVYREPLGV IGIISPWNFP LHLTARSLAP ALALGNACVI
     KPASDTPVTG GLLLAHIFEE AGLPKGVLSV VVGSGSEIGD AFVEHEVPGF ISFTGSTQVG
     RNIGRIAAGG EHLKHVALEL GGNSPFVVLA DADLDQAVNA AVVGKFLHQG QICMAINRII
     VEDSVYDEFV NRYAERVKSL PYGDPSKPET VVGPVINAKQ LAGLQDKIAT AKSEGARVMV
     EGEAQGNVLP PHVFADVTAD MEIAREEIFG PLVGIQRARD EAHALELANS SEYGLSSAVF
     TSSLERGVKF ARGIRAGMTH INDIPVNDEP NAPFGGEKNS GLGRFNGDWA IEEFTTDHWI
     TVQHAPRRYP F