ID A0A2U2ACA5_9GAMM Unreviewed; 419 AA.
AC A0A2U2ACA5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=D-amino acid dehydrogenase {ECO:0000313|EMBL:PWD80291.1};
GN ORFNames=DC083_09710 {ECO:0000313|EMBL:PWD80291.1};
OS Ignatzschineria ureiclastica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Ignatzschineriaceae; Ignatzschineria.
OX NCBI_TaxID=472582 {ECO:0000313|EMBL:PWD80291.1, ECO:0000313|Proteomes:UP000245020};
RN [1] {ECO:0000313|Proteomes:UP000245020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22644 {ECO:0000313|Proteomes:UP000245020};
RA Tsang C.C., Tang J.Y.M., Fong J.Y.H., Kinne J., Lee H.H., Joseph M.,
RA Jose S., Schuster R.K., Tang Y., Sivakumar S., Chen J.H.K., Teng J.L.L.,
RA Lau S.K.P., Wernery U., Woo P.C.Y.;
RT "Ignatzschineria dubaiensis sp. nov., isolated from necrotic foot tissues
RT of dromedaries (Camelus dromedarius) and associated maggots in Dubai,
RT United Arab Emirates.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the DadA oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00009410}.
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:PWD80291.1}.
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DR EMBL; QEWQ01000009; PWD80291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2ACA5; -.
DR OrthoDB; 9805337at2; -.
DR Proteomes; UP000245020; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000245020}.
FT DOMAIN 2..399
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 419 AA; 46184 MW; B104CABFE4F123F6 CRC64;
MDVLVLGSGA VGTSLAYFLA KKGFKVTVVD RQDGAGLETS YGNAGQISPG YASPWAAPGI
PMKAIKWLMQ REHAPLAIRP TKSLKQYHWM WQLLRNCNEK SYATNKARMV RVSEYSRDCL
RDLRKEIDLH YEERTLGTTQ LLRTEAQMQA IQKDIAVLEE FNVPYEVLDR DGIVAVEPAL
AKSVHKLAGG LRLPNDETGD CYLYTSRLAE KAKALGVTFK FGVVVEKIDT DGKKVTGVWV
DGEKLTADAY AVCLGSYGAG KLAPIGIEIP VYPLKGYSLT IPIINPEMAP QSTILDETYK
IAITRFDQRI RVGGMAELMG YDLSLNPRRR ETLEFVTNDL YPEGGNLPEA LFWTGLRPAT
PDGTPILGRA KYENLFLNIG HGTLGWTMAA GSGRYVSDLI AGETPEISSE GLDLSRYHA
//