ID   PADG_AROEV              Reviewed;         417 AA.
AC   Q8L3B1;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=NADH-dependent phenylglyoxylate dehydrogenase subunit alpha;
DE            EC=1.2.1.58;
DE   AltName: Full=Phenylglyoxylate:NAD oxidoreductase;
DE   AltName: Full=Phenylglyoxylate:acceptor oxidoreductase;
GN   Name=padG;
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 14-25, FUNCTION AS A PHENYLGLYOXYLATE DEHYDROGENASE,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP   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   -!- 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}.
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DR   EMBL; AJ428571; CAD21691.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8L3B1; -.
DR   SMR; Q8L3B1; -.
DR   KEGG; ag:CAD21691; -.
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   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN           1..417
FT                   /note="NADH-dependent phenylglyoxylate dehydrogenase
FT                   subunit alpha"
FT                   /id="PRO_0000418535"
SQ   SEQUENCE   417 AA;  45124 MW;  23274BF166F52B07 CRC64;
     MSTATLEKAV AAKAPRKQKV ILAEGNEAAA LGVALARPDM VSVYPITPQS SLVEHVAKLI
     ADGRMDADIV DAEGEHSVLS VLQGGALAGA RTYTATCGPG LAFMFEPYFR TSGMRLPIVL
     TIVTRDGITP QSVWGGHQDA MTVREAGWIQ VYCESVQEVL DTTVMAFKIA EHHDVMLPVN
     VCLDGNYLSY GASRVELPDQ AVVDEFMGEK NVNWHVALDP LRPMAVDPLT GGTTGKGPQT
     FVRYRKGQCR GMQNALSVIE EVHADWAKRI GRSFAPLVEE YRLDDAEFAI MTLGSMTGAA
     KDAVDEAREA GKKIGLIKIK TFSPFPVEAL KKALGKVKAL GVIDRSVGFR WNCGPMYQET
     LGVLYRLGRH IPSISYIGGL AGADITIPHV HRVIDETEAL LNGAVAPTEP VWLNEKD