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

 PADI_AZOEV              Reviewed;         446 AA.
Q8L3A9;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
05-DEC-2018, entry version 54.
RecName: Full=NADH-dependent phenylglyoxylate dehydrogenase subunit beta;
EC=1.2.1.58;
AltName: Full=Phenylglyoxylate:NAD oxidoreductase;
AltName: Full=Phenylglyoxylate:acceptor oxidoreductase;
Name=padI;
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 3-13, FUNCTION AS A PHENYLGLYOXYLATE
DEHYDROGENASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
COFACTOR, ACTIVITY 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:
Reaction=CoA + NAD(+) + phenylglyoxylate = benzoyl-CoA + CO2 +
NADH; Xref=Rhea:RHEA:10372, ChEBI:CHEBI:16526,
ChEBI:CHEBI:36656, ChEBI:CHEBI:57287, ChEBI:CHEBI:57369,
ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.58;
Evidence={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};
-!- ACTIVITY 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; CAD21693.1; -; Genomic_DNA.
ProteinModelPortal; Q8L3A9; -.
SMR; Q8L3A9; -.
KEGG; ag:CAD21693; -.
KO; K18356; -.
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:0047110; F:phenylglyoxylate dehydrogenase (acylating) activity; IDA:UniProtKB.
GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
GO; GO:0006558; P:L-phenylalanine metabolic process; IDA:UniProtKB.
InterPro; IPR017896; 4Fe4S_Fe-S-bd.
InterPro; IPR029061; THDP-binding.
InterPro; IPR011766; TPP_enzyme-bd_C.
Pfam; PF13247; Fer4_11; 1.
Pfam; PF12837; Fer4_6; 1.
Pfam; PF02775; TPP_enzyme_C; 1.
SUPFAM; SSF52518; SSF52518; 1.
PROSITE; PS51379; 4FE4S_FER_2; 4.
1: Evidence at protein level;
4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
NAD; Oxidoreductase; Repeat.
CHAIN 1 446 NADH-dependent phenylglyoxylate
dehydrogenase subunit beta.
/FTId=PRO_0000418537.
DOMAIN 6 35 4Fe-4S ferredoxin-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
DOMAIN 49 80 4Fe-4S ferredoxin-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
DOMAIN 82 111 4Fe-4S ferredoxin-type 3.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
DOMAIN 109 141 4Fe-4S ferredoxin-type 4.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
SEQUENCE 446 AA; 47981 MW; EFCEC3C164D92F50 CRC64;
MGRAYSTIAF DPAKCDGCGD CMTACAQAKT GTDDIARSRI QIYGREGAAD KTFELALCRQ
CADPKCVTVC PAGALNKDGT SGVIGWDATK CVDCLLCTVG CAYAGIALDE ATGHVAKCDT
CDGNPACVPA CPHGALKHIT TANIYNEVGD WEDLFAPGLA GCQGCNTELL MRHTLRRVGP
DTVLATPPGC VPGMGSVGFN GTTGTKVPVF HPLLTNTAAM LAGIKRQYKR VGRDVQALAI
AGDGGASDVG FQSLSGRAER GEQMLFMVVD NEGYMNTGMQ RSSCTPYGAW TSTTPVGETS
RGKTQDAKNL PLIMVNHRCA YVATASTAYM EDLYDKLDKA IAASKNGFAY LHVYSPCTTA
WRFPSNLNME VARKAVETNF VMLWEYTPQD GLHFTKPVDD PLPVTDYLKA MGRFRHLTPE
QVEHIQKKVV ENQKFVERMT EHAHVG


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EIAAB26756 Cell adhesion protein SQM1,CI-B18,Complex I-B18,Homo sapiens,Human,NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7,NADH-ubiquinone oxidoreductase B18 subunit,NDUFB7
EIAAB26818 Bos taurus,Bovine,NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial,NADH dehydrogenase subunit II,NADH-ubiquinone oxidoreductase 24 kDa subunit,NDUFV2
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