XYLC_PSEPU
ID XYLC_PSEPU Reviewed; 487 AA.
AC P43503;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Benzaldehyde dehydrogenase [NAD(+)];
DE EC=1.2.1.28;
GN Name=xylC;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid TOL pWW0, and Plasmid TOL pWW53.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15.
RC PLASMID=TOL pWW0;
RX PubMed=7868591; DOI=10.1128/jb.177.5.1196-1201.1995;
RA Inoue J., Shaw J.P., Rekik M., Harayama S.;
RT "Overlapping substrate specificities of benzaldehyde dehydrogenase (the
RT xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the
RT xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida.";
RL J. Bacteriol. 177:1196-1201(1995).
RN [2]
RP PROTEIN SEQUENCE OF 1-53.
RC PLASMID=TOL pWW53;
RX PubMed=1989592; DOI=10.1042/bj2730099;
RA Chalmers R.M., Keen J.N., Fewson C.A.;
RT "Comparison of benzyl alcohol dehydrogenases and benzaldehyde
RT dehydrogenases from the benzyl alcohol and mandelate pathways in
RT Acinetobacter calcoaceticus and from the TOL-plasmid-encoded toluene
RT pathway in Pseudomonas putida. N-terminal amino acid sequences, amino acid
RT compositions and immunological cross-reactions.";
RL Biochem. J. 273:99-107(1991).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:11840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.28;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0.;
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U15151; AAA66218.1; -; Genomic_DNA.
DR EMBL; D63341; BAA09661.1; -; Genomic_DNA.
DR PIR; T47107; T47107.
DR RefSeq; NP_542888.1; NC_003350.1.
DR RefSeq; WP_011005931.1; NZ_QWEF01000005.1.
DR AlphaFoldDB; P43503; -.
DR SMR; P43503; -.
DR KEGG; ag:AAA66218; -.
DR BioCyc; MetaCyc:MON-2968; -.
DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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 Aromatic hydrocarbons catabolism; Direct protein sequencing; NAD;
KW Oxidoreductase; Plasmid.
FT CHAIN 1..487
FT /note="Benzaldehyde dehydrogenase [NAD(+)]"
FT /id="PRO_0000056591"
FT ACT_SITE 254
FT /evidence="ECO:0000250"
FT ACT_SITE 288
FT /evidence="ECO:0000250"
FT BINDING 232..237
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 487 AA; 51897 MW; 093CB3E9487AF384 CRC64;
MRETKEQPIW YGKVFSSNWV EARGGVANVV DPSNGDILGI TGVANGEDVD AAVNAAKRAQ
KEWAAIPFSE RAAIVRKAAE KLKEREYEFA DWNVRECGAI RPKGLWEAGI AYEQMHQAAG
LASLPNGTLF PSAVPGRMNL CQRVPVGVVG VIAPWNFPLF LAMRSVAPAL ALGNAVILKP
DLQTAVTGGA LIAEIFSDAG MPDGVLHVLP GGADVGESMV ANSGINMISF TGSTQVGRLI
GEKCGRMLKK VALELGGNNV HIVLPDADLE GAVSCAAWGT FLHQGQVCMA AGRHLVHRDV
AQQYAEKLAL RAKNLVVGDP NSDQVHLGPL INEKQVVRVH ALVESAQRAG AQVLAGGTYQ
DRYYQATVIM DVKPEMEVFK SEIFGPVAPI TVFDSIEEAI ELANCSEYGL AASIHTRALA
TGLDIAKRLN TGMVHINDQP INCEPHVPFG GMGASGSGGR FGGPASIEEF TQSQWISMVE
KPANYPF