PADH_AROEV
ID PADH_AROEV Reviewed; 421 AA.
AC Q8L3B0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=NADH-dependent phenylglyoxylate dehydrogenase subunit epsilon;
DE EC=1.2.1.58;
DE AltName: Full=Phenylglyoxylate:NAD oxidoreductase;
DE AltName: Full=Phenylglyoxylate:acceptor oxidoreductase;
GN Name=padH;
OS Aromatoleum evansii (Azoarcus evansii).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=59406;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6898 / NBRC 107771 / KB740;
RA Haas S., Hammer E., Herrmann H., Burchhardt G.;
RT "Characterization of genes involved in anaerobic phenylacetate degradation
RT in Azoarcus evansii.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 1-12, FUNCTION AS A PHENYLGLYOXYLATE DEHYDROGENASE,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY
RP REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT, AND INDUCTION.
RC STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX PubMed=9490067; DOI=10.1046/j.1432-1327.1998.2510907.x;
RA Hirsch W., Schagger H., Fuchs G.;
RT "Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme of
RT anaerobic phenylalanine metabolism in the denitrifying bacterium Azoarcus
RT evansii.";
RL Eur. J. Biochem. 251:907-915(1998).
CC -!- FUNCTION: Involved in the anaerobic metabolism of phenylalanine and
CC phenylacetate. Catalyzes the oxidative decarboxylation of
CC phenylglyoxylate to benzoyl-CoA and CO(2). It can also react slowly
CC with 2-oxo-3-methylbutanoate and use different electron acceptors such
CC as benzyl viologen, methyl viologen, FAD or FMN, but NAD seems to be
CC the physiological electron acceptor. Also catalyzes an isotope exchange
CC between CO(2) and the carboxyl group which proves partial or complete
CC reversibility of the oxidative decarboxylation reaction.
CC {ECO:0000269|PubMed:9490067}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + NAD(+) + phenylglyoxylate = benzoyl-CoA + CO2 + NADH;
CC Xref=Rhea:RHEA:10372, ChEBI:CHEBI:16526, ChEBI:CHEBI:36656,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57369, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.58;
CC Evidence={ECO:0000269|PubMed:9490067};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:9490067};
CC -!- ACTIVITY REGULATION: Activated by magnesium ions and thiamine
CC diphosphate. {ECO:0000269|PubMed:9490067}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45 uM for phenylglyoxylate (under anaerobic conditions at 37
CC degrees Celsius and pH 7.8) {ECO:0000269|PubMed:9490067};
CC KM=55 uM for coenzyme-A (under anaerobic conditions at 37 degrees
CC Celsius and pH 7.8) {ECO:0000269|PubMed:9490067};
CC KM=74 uM for NAD (under anaerobic conditions at 37 degrees Celsius
CC and pH 7.8) {ECO:0000269|PubMed:9490067};
CC pH dependence:
CC Optimum pH is 8 when measured with benzyl viologen. Half-maximal
CC activities are obtained at pH 9 and pH 6.8.
CC {ECO:0000269|PubMed:9490067};
CC -!- SUBUNIT: Dimer of heteropentamers composed of an alpha (PadG), a beta
CC (PadI), a gamma (PadE), a delta (PadF) and an epsilon (PadH) subunit.
CC {ECO:0000269|PubMed:9490067}.
CC -!- INDUCTION: Induced anaerobically by phenylalanine, phenylacetate or
CC phenylglyoxylate. {ECO:0000269|PubMed:9490067}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AJ428571; CAD21692.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8L3B0; -.
DR SMR; Q8L3B0; -.
DR KEGG; ag:CAD21692; -.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0047110; F:phenylglyoxylate dehydrogenase (acylating) activity; IDA:UniProtKB.
DR GO; GO:0006558; P:L-phenylalanine metabolic process; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidoreductase.
FT CHAIN 1..421
FT /note="NADH-dependent phenylglyoxylate dehydrogenase
FT subunit epsilon"
FT /id="PRO_0000418539"
FT BINDING 15..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 39..40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 279..297
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 421 AA; 44864 MW; A6B665ECB3DD7F68 CRC64;
MDRAIEHTKY LIAGSSHAAL EAINAIRMHD AEGPITVVTR DAHLPYSPTV LPYVVSGKSA
PERIFLRDDD FFARNKVAYR PKAALKALHA DRNTAELADG SSVVYEKLLL ATGASPAIPP
IPGIDTVSYH VLRTLDDALK LRGAIAESKQ AVVLGAGLVG MHAAENLVKA GATVTIVEMS
EQLTSGYFDK VAADMIEQAF RDAGGKIMTG SRVVRLEPTA AGAKLTLENG TTLEADLLLV
ATGVKPEMDY LNGSGVEHAQ GILVDDRMQT TAENVWAAAT AQARGFFTGT KVMNAILPDA
TIQGRVAGMA MAGDPGVKDY AGAVPLNTYH FFGRHAISVG SSTVPEGGEV VTRFDEKTGR
YLKAIFAADG PLTGIFGVNE FFDGGVMAQL ILRRTDLTPL RSRFVANPLA VGREIMSQTW
R
