PADI_AROEV
ID PADI_AROEV Reviewed; 446 AA.
AC Q8L3A9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=NADH-dependent phenylglyoxylate dehydrogenase subunit beta;
DE EC=1.2.1.58;
DE AltName: Full=Phenylglyoxylate:NAD oxidoreductase;
DE AltName: Full=Phenylglyoxylate:acceptor oxidoreductase;
GN Name=padI;
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 3-13, 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000305|PubMed:9490067};
CC Note=Binds 3 [4Fe-4S] clusters per heteropentamers.
CC {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}.
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DR EMBL; AJ428571; CAD21693.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8L3A9; -.
DR SMR; Q8L3A9; -.
DR PRIDE; Q8L3A9; -.
DR KEGG; ag:CAD21693; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0047110; F:phenylglyoxylate dehydrogenase (acylating) activity; IDA:UniProtKB.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006558; P:L-phenylalanine metabolic process; IDA:UniProtKB.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR Pfam; PF13247; Fer4_11; 1.
DR Pfam; PF12837; Fer4_6; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; NAD;
KW Oxidoreductase; Repeat.
FT CHAIN 1..446
FT /note="NADH-dependent phenylglyoxylate dehydrogenase
FT subunit beta"
FT /id="PRO_0000418537"
FT DOMAIN 6..35
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 49..80
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 82..111
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 109..141
FT /note="4Fe-4S ferredoxin-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ 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
