ID   DADA_HELPY              Reviewed;         410 AA.
AC   O25597;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=D-amino acid dehydrogenase {ECO:0000250|UniProtKB:A3KEZ1};
DE            Short=DAD {ECO:0000250|UniProtKB:A3KEZ1};
DE            EC=1.4.5.1 {ECO:0000250|UniProtKB:A3KEZ1};
GN   Name=dadA {ECO:0000250|UniProtKB:A3KEZ1}; OrderedLocusNames=HP_0943;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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:0000250|UniProtKB:A3KEZ1}.
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:0000250|UniProtKB:A3KEZ1};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:A3KEZ1};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:A3KEZ1}; Peripheral membrane protein
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DadA oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AE000511; AAD07988.1; -; Genomic_DNA.
DR   PIR; G64637; G64637.
DR   RefSeq; NP_207735.1; NC_000915.1.
DR   RefSeq; WP_000712480.1; NC_018939.1.
DR   AlphaFoldDB; O25597; -.
DR   SMR; O25597; -.
DR   STRING; 85962.C694_04855; -.
DR   PaxDb; O25597; -.
DR   DNASU; 899472; -.
DR   EnsemblBacteria; AAD07988; AAD07988; HP_0943.
DR   KEGG; hpy:HP_0943; -.
DR   PATRIC; fig|85962.47.peg.1009; -.
DR   eggNOG; COG0665; Bacteria.
DR   OMA; FWYKEDG; -.
DR   PhylomeDB; O25597; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Electron transport; FAD; Flavoprotein;
KW   Membrane; Oxidoreductase; Reference proteome; Transport.
FT   CHAIN           1..410
FT                   /note="D-amino acid dehydrogenase"
FT                   /id="PRO_0000166162"
FT   BINDING         9..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A3KEZ1"
SQ   SEQUENCE   410 AA;  46113 MW;  8F4EC7349C93CC91 CRC64;
     MKKEVVVIGG GIVGLSCAYS MHKLGHKVCV IEKNDGANGT SFGNAGLISA FKKAPLSCPG
     VVLDTLKLML KNQAPLKFHF GLNLKLYQWI LKFVKSANAK STHRTMALFE RYGWLSIDMY
     HQMLKDGMDF WYKEDGLLMI YTLEESFEKK LKTCDNSGAY KILSAKETKE YMPVVNDNIC
     GSVLLTENAH VDPGEVMHSL QEYLQNVGVE FLYNEEVIDF EFKNNLIEGV ITHKEKIQAE
     TIILATGANP TLIKKTKNDF LMMGAKGYSI TFKMPEELKP KTSSLFADIF MAMTPRRDTV
     RITSKLELNT NNALIDKEQI ANMKKNLAAF TQPFEMKDAI EWCGFRPLTP NDIPYLGYDK
     RYKNLIHATG LGWLGITFGP AIGKIIANLS QDGANEKNAD IMLFSAFFRD