ID A0A0L0APD0_9ENTR Unreviewed; 432 AA.
AC A0A0L0APD0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=D-amino acid dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01202};
DE EC=1.4.99.- {ECO:0000256|HAMAP-Rule:MF_01202};
GN Name=dadA {ECO:0000256|HAMAP-Rule:MF_01202};
GN ORFNames=AC791_13250 {ECO:0000313|EMBL:KNC09601.1};
OS Klebsiella sp. RIT-PI-d.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1681196 {ECO:0000313|EMBL:KNC09601.1, ECO:0000313|Proteomes:UP000053401};
RN [1] {ECO:0000313|Proteomes:UP000053401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT-PI-d {ECO:0000313|Proteomes:UP000053401};
RA Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT "Whole genome sequencing of endophytes isolated from poison ivy
RT (Toxicodendron radicans).";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxidative deamination of D-amino acids. {ECO:0000256|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:0000256|ARBA:ARBA00000728,
CC ECO:0000256|HAMAP-Rule:MF_01202};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_01202};
CC -!- PATHWAY: Amino-acid degradation; D-alanine degradation; NH(3) and
CC pyruvate from D-alanine: step 1/1. {ECO:0000256|ARBA:ARBA00004960}.
CC -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00009410, ECO:0000256|HAMAP-Rule:MF_01202}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC09601.1}.
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DR EMBL; LGIT01000009; KNC09601.1; -; Genomic_DNA.
DR RefSeq; WP_049840885.1; NZ_LGIT01000009.1.
DR AlphaFoldDB; A0A0L0APD0; -.
DR STRING; 1681196.AC791_13250; -.
DR PATRIC; fig|1681196.3.peg.1505; -.
DR OrthoDB; 9805337at2; -.
DR UniPathway; UPA00043; UER00498.
DR Proteomes; UP000053401; Unassembled WGS sequence.
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; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 InterPro; IPR001763; Rhodanese-like_dom.
DR PANTHER; PTHR13847:SF280; D-AMINO ACID DEHYDROGENASE; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|HAMAP-Rule:MF_01202};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01202};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01202,
KW ECO:0000313|EMBL:KNC09601.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053401}.
FT DOMAIN 3..39
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01202"
SQ SEQUENCE 432 AA; 47449 MW; FE3F8D4EDE741FCA CRC64;
MHVVVLGSGV VGVTSAWYLR QAGHDVTVID RAAGPALETS AANAGQISPG YAAPWAAPGV
PLKAIKWMFQ RHAPLAVSLD GSSFQLKWMW QMLRNCDTRH YMENKGRMVR LAEYSRDCLR
TLRADTGIQY EGRQGGTLQL FRTAQQYENA ARDIAVLKDA GVPYQLLEAR DLAQIEPALG
GVSHRLTGGL RLPNDETGDC QLFSQRLAEM AEQAGVVFRY NMSVDRLLYE SNKIYGVKCG
DNIIKADAYV MAFGSYSTTM LKGLMDIPVY PLKGYSLTIP IDDESGAPVS TILDETYKIA
ITRFEQRIRV GGMAEIVGFN TRLLPPRRET LEMVVRDLFP RGGHVEQATF WTGLRPMTPD
GTPIVGRTPF KNLWLNTGHG TLGWTMACGS GQLISDLISG RTPAIPFDDL GVARYSAGFR
PSTPAHLHGA HS
//
