DADA_HELPJ
ID DADA_HELPJ Reviewed; 410 AA.
AC Q9ZKQ7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=jhp_0878;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD06449.1; -; Genomic_DNA.
DR PIR; H71877; H71877.
DR RefSeq; WP_000712569.1; NC_000921.1.
DR AlphaFoldDB; Q9ZKQ7; -.
DR SMR; Q9ZKQ7; -.
DR STRING; 85963.jhp_0878; -.
DR EnsemblBacteria; AAD06449; AAD06449; jhp_0878.
DR KEGG; hpj:jhp_0878; -.
DR eggNOG; COG0665; Bacteria.
DR OMA; FWYKEDG; -.
DR Proteomes; UP000000804; Chromosome.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; FAD; Flavoprotein;
KW Membrane; Oxidoreductase; Transport.
FT CHAIN 1..410
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_0000166163"
FT BINDING 9..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A3KEZ1"
SQ SEQUENCE 410 AA; 46102 MW; D8BD6A787E2B7695 CRC64;
MKKEVVVIGG GIVGLSCAYS MHKLGHKVCV IEKSDGTNGT SFGNAGLISA FKKAPLSCPG
VVLDTLKLML KNQAPLKFHF GLNLKLYQWI LKFMTSANAK STHRTIALFE RYGWLSIDMY
HQMLKDGMDF WYKEDGLLMI YTLEESFEKK LKTCDNSGAY KILNVKETKE YMPIANDNIC
GSVLLTENAH VDPGEVVRSL QQYLQNAGVE FLYNEEVIDF EFKNNLIEGV ITHKEKIQAE
TIILATGANP TLIKKTKNDF LMMGAKGYSI TFKMPEELKP KTSSLFADIF MAMTPRRDTV
RITSKLELNT NNALIDKEQI ANMKKNLAAF TQPFEMKDAI EWCGFRPLTP NDIPYLGYDK
RYKNLIHATG LGWLGITFGP AIGKIIANLS QDGANEKNAD IMLFSAFFRD
