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NADH-dependent phenylglyoxylate dehydrogenase subunit delta (EC 1.2.1.58) (Phenylglyoxylate:NAD oxidoreductase) (Phenylglyoxylate:acceptor oxidoreductase)

 PADF_AZOEV              Reviewed;          93 AA.
Q8L3B2;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
20-DEC-2017, entry version 54.
RecName: Full=NADH-dependent phenylglyoxylate dehydrogenase subunit delta;
EC=1.2.1.58;
AltName: Full=Phenylglyoxylate:NAD oxidoreductase;
AltName: Full=Phenylglyoxylate:acceptor oxidoreductase;
Name=padF;
Azoarcus evansii.
Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
Zoogloeaceae; Azoarcus.
NCBI_TaxID=59406;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=KB740 / DSM 6898;
Haas S., Hammer E., Herrmann H., Burchhardt G.;
"Characterization of genes involved in anaerobic phenylacetate
degradation in Azoarcus evansii.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 2-13, FUNCTION AS A PHENYLGLYOXYLATE
DEHYDROGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
COFACTOR, ENZYME REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT, AND
INDUCTION.
STRAIN=KB740 / DSM 6898;
PubMed=9490067; DOI=10.1046/j.1432-1327.1998.2510907.x;
Hirsch W., Schagger H., Fuchs G.;
"Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme
of anaerobic phenylalanine metabolism in the denitrifying bacterium
Azoarcus evansii.";
Eur. J. Biochem. 251:907-915(1998).
-!- FUNCTION: Involved in the anaerobic metabolism of phenylalanine
and phenylacetate. Catalyzes the oxidative decarboxylation of
phenylglyoxylate to benzoyl-CoA and CO(2). It can also react
slowly with 2-oxo-3-methylbutanoate and use different electron
acceptors such as benzyl viologen, methyl viologen, FAD or FMN,
but NAD seems to be the physiological electron acceptor. Also
catalyzes an isotope exchange between CO(2) and the carboxyl group
which proves partial or complete reversibility of the oxidative
decarboxylation reaction. {ECO:0000269|PubMed:9490067}.
-!- CATALYTIC ACTIVITY: Phenylglyoxylate + NAD(+) + CoA = benzoyl-S-
CoA + CO(2) + NADH. {ECO:0000269|PubMed:9490067}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000305|PubMed:9490067};
Note=Binds 3 [4Fe-4S] clusters per heteropentamers.
{ECO:0000305|PubMed:9490067};
-!- ENZYME REGULATION: Activated by magnesium ions and thiamine
diphosphate. {ECO:0000269|PubMed:9490067}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=45 uM for phenylglyoxylate (under anaerobic conditions at 37
degrees Celsius and pH 7.8) {ECO:0000269|PubMed:9490067};
KM=55 uM for coenzyme-A (under anaerobic conditions at 37
degrees Celsius and pH 7.8) {ECO:0000269|PubMed:9490067};
KM=74 uM for NAD (under anaerobic conditions at 37 degrees
Celsius and pH 7.8) {ECO:0000269|PubMed:9490067};
pH dependence:
Optimum pH is 8 when measured with benzyl viologen. Half-maximal
activities are obtained at pH 9 and pH 6.8.
{ECO:0000269|PubMed:9490067};
-!- SUBUNIT: Dimer of heteropentamers composed of an alpha (PadG), a
beta (PadI), a gamma (PadE), a delta (PadF) and an epsilon (PadH)
subunit. {ECO:0000269|PubMed:9490067}.
-!- INDUCTION: Induced anaerobically by phenylalanine, phenylacetate
or phenylglyoxylate. {ECO:0000269|PubMed:9490067}.
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EMBL; AJ428571; CAD21690.1; -; Genomic_DNA.
ProteinModelPortal; Q8L3B2; -.
SMR; Q8L3B2; -.
KEGG; ag:CAD21690; -.
KO; K18358; -.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro.
GO; GO:0047110; F:phenylglyoxylate dehydrogenase (acylating) activity; IDA:UniProtKB.
GO; GO:0006558; P:L-phenylalanine metabolic process; IDA:UniProtKB.
InterPro; IPR017896; 4Fe4S_Fe-S-bd.
InterPro; IPR017900; 4Fe4S_Fe_S_CS.
InterPro; IPR011898; PorD_KorD.
PANTHER; PTHR43724; PTHR43724; 1.
Pfam; PF00037; Fer4; 1.
TIGRFAMs; TIGR02179; PorD_KorD; 1.
PROSITE; PS00198; 4FE4S_FER_1; 2.
PROSITE; PS51379; 4FE4S_FER_2; 2.
1: Evidence at protein level;
4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
NAD; Oxidoreductase; Repeat.
CHAIN 1 93 NADH-dependent phenylglyoxylate
dehydrogenase subunit delta.
/FTId=PRO_0000418538.
DOMAIN 39 68 4Fe-4S ferredoxin-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
DOMAIN 66 93 4Fe-4S ferredoxin-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
SEQUENCE 93 AA; 10564 MW; 4AB5967CB39A6C1B CRC64;
MSRHQSYPLF NLEQAGVPDD LCPVATVVSP MLPGDWRSMR PVVDRDKCVK CAVCWLYCPV
QCVEEHAAWF DFNLKTCKGC GICANECPQR RSR


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