DADA_PHOLL
ID DADA_PHOLL Reviewed; 436 AA.
AC Q7N3Z6;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=D-amino acid dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01202};
DE EC=1.4.99.- {ECO:0000255|HAMAP-Rule:MF_01202};
GN Name=dadA {ECO:0000255|HAMAP-Rule:MF_01202}; OrderedLocusNames=plu2561;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
CC -!- FUNCTION: Oxidative deamination of D-amino acids. {ECO:0000255|HAMAP-
CC Rule:MF_01202}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + a D-alpha-amino acid + H2O = a 2-oxocarboxylate + AH2 +
CC NH4(+); Xref=Rhea:RHEA:18125, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59871; Evidence={ECO:0000255|HAMAP-Rule:MF_01202};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01202};
CC -!- PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and
CC pyruvate from D-alanine: step 1/1.
CC -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC {ECO:0000255|HAMAP-Rule:MF_01202}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE14935.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX571867; CAE14935.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041380099.1; NC_005126.1.
DR AlphaFoldDB; Q7N3Z6; -.
DR SMR; Q7N3Z6; -.
DR STRING; 243265.plu2561; -.
DR EnsemblBacteria; CAE14935; CAE14935; plu2561.
DR GeneID; 24166099; -.
DR KEGG; plu:plu2561; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_6; -.
DR OMA; FWYKEDG; -.
DR OrthoDB; 573710at2; -.
DR BioCyc; PLUM243265:PLU_RS12680-MON; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000002514; Chromosome.
DR GO; GO:0008718; F:D-amino-acid dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0055130; P:D-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 2.
DR HAMAP; MF_01202; DadA; 1.
DR InterPro; IPR023080; DadA.
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 FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..436
FT /note="D-amino acid dehydrogenase"
FT /id="PRO_0000166137"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01202"
SQ SEQUENCE 436 AA; 47971 MW; 24216B33BF0B331C CRC64;
MKILILGSGV IGVTSAWYLV QQGHEVTVID RQGSAAEETS AANAGQISPG YATPWGAPGI
PLKAIKWMFQ RHAPLAIRPD GSLFQLRWMW QMLRNCDASH YAINKSRMVR LAEYSRDCIK
QLRADTGIQY EGRQRGTLQL FRTNKQFDNA VNDIAVLEQE GVPYNLLTAD KLATVEPALA
HAAHKLTGGL QLPNDETGDC QLFTKELVKM AEAAGVTFLF NKQVKQLLVE GHRIIGVQCE
DGVMTADNYV VAMGAYSTEL LKGLVKIPVY PLKGYSLTMP IVDAERAPVS TALDETYKIA
ITRFDNRIRV GGMAEVVGFN LNLLKARHET LKMVVQDLYP GGGDITQTHF WTGLRPMTPD
GTPIVGPTEY HNLYLNTGHG TLGWTMACGS SQLLADIISG KKPAIASDDL SVFRYVNGFN
TKLVPFSHQL HTELRG
