DADA_HELPX
ID DADA_HELPX Reviewed; 410 AA.
AC A3KEZ1;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=D-amino acid dehydrogenase {ECO:0000303|PubMed:19212808};
DE Short=DAD {ECO:0000303|PubMed:19212808};
DE EC=1.4.5.1 {ECO:0000269|PubMed:19212808};
GN Name=dadA {ECO:0000303|PubMed:19212808};
OS Helicobacter pylori (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=210;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10 AND 193-197,
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RX PubMed=19212808; DOI=10.1007/s00726-009-0240-0;
RA Tanigawa M., Shinohara T., Saito M., Nishimura K., Hasegawa Y.,
RA Wakabayashi S., Ishizuka M., Nagata Y.;
RT "D-Amino acid dehydrogenase from Helicobacter pylori NCTC 11637.";
RL Amino Acids 38:247-255(2010).
CC -!- FUNCTION: Catalyzes the oxidative deamination of D-amino acids. Has
CC broad substrate specificity; is mostly active on D-proline, and to a
CC lesser extent, on several other D-amino acids such as D-alanine, D-
CC phenylalanine and D-serine. Mediates electron transport from D-proline
CC to coenzyme Q1 in vitro, and is involved in the electron transport
CC chain from D-proline to the c-type cytochrome in vivo.
CC {ECO:0000269|PubMed:19212808}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-alpha-amino acid + a quinone + H2O = a 2-oxocarboxylate +
CC a quinol + NH4(+); Xref=Rhea:RHEA:45996, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59871, ChEBI:CHEBI:132124; EC=1.4.5.1;
CC Evidence={ECO:0000269|PubMed:19212808};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:19212808};
CC -!- ACTIVITY REGULATION: Activity is markedly inhibited by benzoate, and
CC moderately by SH reagents such as p-hydroxymercuribenzoate,
CC iodoacetamide, and iodoacetate. {ECO:0000269|PubMed:19212808}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40.2 mM for D-proline {ECO:0000269|PubMed:19212808};
CC KM=60.0 mM for D-alanine {ECO:0000269|PubMed:19212808};
CC KM=8.2 uM for coenyzme Q1 {ECO:0000269|PubMed:19212808};
CC KM=5.3 mM for DCIP {ECO:0000269|PubMed:19212808};
CC Vmax=25 umol/min/mg enzyme with D-proline as the electron donor and
CC coenyzme Q1 as the electron acceptor {ECO:0000269|PubMed:19212808};
CC Vmax=18.3 umol/min/mg enzyme with D-alanine as the electron donor and
CC coenyzme Q1 as the electron acceptor {ECO:0000269|PubMed:19212808};
CC Vmax=4.5 umol/min/mg enzyme with D-proline as the electron donor and
CC DCIP as the electron acceptor {ECO:0000269|PubMed:19212808};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:19212808};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:19212808};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:19212808,
CC ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DadA oxidoreductase family. {ECO:0000305}.
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DR EMBL; AB295062; BAF48065.1; -; Genomic_DNA.
DR RefSeq; WP_000712537.1; NZ_JAFCIE010000017.1.
DR AlphaFoldDB; A3KEZ1; -.
DR SMR; A3KEZ1; -.
DR STRING; 1345592.CBOM010000017_gene1226; -.
DR KEGG; ag:BAF48065; -.
DR eggNOG; COG0665; Bacteria.
DR BioCyc; MetaCyc:MON-15373; -.
DR BRENDA; 1.4.5.1; 2604.
DR BRENDA; 1.4.99.6; 2604.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Electron transport; FAD; Flavoprotein; Membrane; Oxidoreductase; Transport.
FT CHAIN 1..410
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_0000430690"
FT BINDING 9..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000303|PubMed:19212808"
SQ SEQUENCE 410 AA; 46041 MW; B3C8C5EE0B3F6BE6 CRC64;
MKKEVVVIGG GIVGLSCAYS MHKLGHKVCV IEKSDGANGT SFGNAGLISA FKKAPLSCPG
VVLDTLKLML KNQAPLKFHF GLNLKLYQWI LKFVKSANAK STHRTMALFE RYGWLSVDIY
HQMLKDGMDF WYKEDGLLMI YTLEESFEKK LKTCDDSGAY KILSAKETKE YMPIVNDNIC
GSVLLTENAH VDPGEVMHSL QEYLQNAGVE FLYNEEVIDF EFKNNLIEGV ITHKEKIQAE
TIILATGANP TLIKKTKNDF LMMGAKGYSI TFKMPEELKP KTSSLFADIF MAMTPRRDTV
RITSKLELNT NNALIDKEQI ANMKKNLAAF TQPFEMKDAI EWCGFRPLTP NDIPYLGYDK
RYKNLIHATG LGWLGITFGP AIGKIIANLS QDGANEKNAD IMLFSAFFRD
