PHDK_NOCSK
ID PHDK_NOCSK Reviewed; 485 AA.
AC Q79EM7; O24724;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=2-formylbenzoate dehydrogenase {ECO:0000303|PubMed:9335300, ECO:0000305|PubMed:9335300};
DE EC=1.2.1.78 {ECO:0000269|PubMed:9335300};
DE AltName: Full=2-carboxybenzaldehyde dehydrogenase {ECO:0000303|PubMed:9335300, ECO:0000312|EMBL:BAA31236.1};
DE Short=2-CBAL dehydrogenase {ECO:0000305|PubMed:9335300};
DE AltName: Full=2-formylbenzoate:NAD(+) oxidoreductase {ECO:0000305|PubMed:9335300};
GN Name=phdK {ECO:0000312|EMBL:BAA31236.1};
OS Nocardioides sp. (strain KP7).
OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC Nocardioides.
OX NCBI_TaxID=102632;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA31236.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-30, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
RX PubMed=9335300; DOI=10.1128/jb.179.20.6488-6494.1997;
RA Iwabuchi T., Harayama S.;
RT "Biochemical and genetic characterization of 2-carboxybenzaldehyde
RT dehydrogenase, an enzyme involved in phenanthrene degradation by
RT Nocardioides sp. strain KP7.";
RL J. Bacteriol. 179:6488-6494(1997).
CC -!- FUNCTION: Plays a role in phenanthrene catabolism by catalyzing the
CC oxidation of 2-carboxybenzaldehyde to phthalic acid. Not active with 3-
CC carboxybenzaldehyde, 4-carboxybenzaldehyde, benzaldehyde,
CC salicylaldehyde, 2-methylbenzaldehyde, 2-chlorobenzaldehyde, 2-
CC fluorobenzaldehyde, 2-benzaldehydesulfonate, 2-methoxybenzaldehyde, 1-
CC hydroxy-2-naphthoaldehyde or n-hexylaldehyde.
CC {ECO:0000269|PubMed:9335300}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-formylbenzoate + H2O + NAD(+) = 2 H(+) + NADH + phthalate;
CC Xref=Rhea:RHEA:27298, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17563, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58203; EC=1.2.1.78;
CC Evidence={ECO:0000269|PubMed:9335300};
CC -!- ACTIVITY REGULATION: Inhibited weakly by Mn(2+), Mg(2+) and Ca(2+), but
CC not affected by Zn(2+), Co(2+), Cu(2+), EDTA or EGTA.
CC {ECO:0000269|PubMed:9335300}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=100 uM for 2-carboxybenzaldehyde {ECO:0000269|PubMed:9335300};
CC KM=83 uM for NAD(+) {ECO:0000269|PubMed:9335300};
CC KM=28 mM for 2-nitrobenzaldehyde {ECO:0000269|PubMed:9335300};
CC Note=kcat is 39 sec(-1) with 2-carboxybenzaldehyde as substrate. kcat
CC is 32 sec(-1) with NAD as substrate.;
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:9335300};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:9335300};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9335300}.
CC -!- INDUCTION: By phenanthrene. {ECO:0000269|PubMed:9335300}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255}.
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DR EMBL; AB000735; BAA23265.1; -; Genomic_DNA.
DR EMBL; D89989; BAA31236.1; -; Genomic_DNA.
DR AlphaFoldDB; Q79EM7; -.
DR SMR; Q79EM7; -.
DR KEGG; ag:BAA23265; -.
DR BRENDA; 1.2.1.78; 4363.
DR GO; GO:0018474; F:2-carboxybenzaldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0042216; P:phenanthrene 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; 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 Aromatic hydrocarbons catabolism; Direct protein sequencing; NAD;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9335300"
FT CHAIN 2..485
FT /note="2-formylbenzoate dehydrogenase"
FT /evidence="ECO:0000269|PubMed:9335300"
FT /id="PRO_0000421855"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q28399,
FT ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 288
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q28399,
FT ECO:0000255|PROSITE-ProRule:PRU10007"
FT BINDING 229..234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q28399"
FT CONFLICT 18
FT /note="G -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000269|PubMed:9335300"
FT CONFLICT 30
FT /note="S -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000269|PubMed:9335300"
SQ SEQUENCE 485 AA; 51806 MW; E97EB6854CCDB523 CRC64;
MTTPRKFDEY RWNVLVDGVP LNVESRYPIS DPSTGRYLTQ VPDCAEADVD RAVQASRQAQ
AEWGALPPRA RAAKLRELIT LLREHREEFA MLDAIDGGFP ISMMRNDVDA ALELMDIFAD
MALDLGGKTI PVSTNLHFTT HEPFGVVARI GAFNHPFFFA ASKVAAPLMA GNSVILKAPD
QTPLSSLRLA EVAAEVLPQN LLITISGRGR VAGRAIVRHP QIKRIGFIGS TDTGRSIQRD
AAEVAVKHIS LELGGKNAQI VFADADLEQA ALGAVNGMNF TWTAGQSCGS TSRLLVHESV
ADQVIARVVE LVSAIAVGPP LDENAQMGPL VSQAQYDKSV HAIGEGIREG AKVVAGGGRP
EGVGEGGWYL APTVLADVRP GSFIEQNEIF GPVLSVIIFA TDDEAVAIAN GVEYGLTASV
WTSDITRAHL IARRVEAGYV LVNGGSRHYW GLPFGGVKSS GVGSEESMEE LISYTETKTT
TVVLG
