ID   A0A0Q4CG68_9SPHN        Unreviewed;       412 AA.
AC   A0A0Q4CG68;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:KQM23884.1};
GN   ORFNames=ASE58_16450 {ECO:0000313|EMBL:KQM23884.1};
OS   Sphingomonas sp. Leaf9.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1735674 {ECO:0000313|EMBL:KQM23884.1, ECO:0000313|Proteomes:UP000051210};
RN   [1] {ECO:0000313|EMBL:KQM23884.1, ECO:0000313|Proteomes:UP000051210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf9 {ECO:0000313|EMBL:KQM23884.1,
RC   ECO:0000313|Proteomes:UP000051210};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM23884.1, ECO:0000313|Proteomes:UP000051210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf9 {ECO:0000313|EMBL:KQM23884.1,
RC   ECO:0000313|Proteomes:UP000051210};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQM23884.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMKC01000006; KQM23884.1; -; Genomic_DNA.
DR   RefSeq; WP_055823774.1; NZ_LMKC01000006.1.
DR   AlphaFoldDB; A0A0Q4CG68; -.
DR   OrthoDB; 9805337at2; -.
DR   Proteomes; UP000051210; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; SSF51971; Nucleotide-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          6..393
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   412 AA;  42975 MW;  64EFFD6D3593840D CRC64;
     MTATAIVIGD GVVALNVALA LQRRGTQVTI VAPDAPWRGA SWGNAGHIAV EQVEPLASLA
     TVTSVPKRLF SRGGALALPP RAIRTWLPFT LRLLRAAAPA RFARGKVALS AMLATAIPAW
     QRVLAAAGRG DLLRIAGHFV VWETPESAAR GQAAWAAADT GTATVRPVTP DELARLQTLT
     TVPIAGAIRF EGSGQIVDPA ALGAALLGQF VANGGTMIRT RARARAIVEA DGGARVVLEQ
     GAPIEAAVAV VAAGAASAAL VKAVGLTAPL IAERGYHVEG DPGEWPADLP PVVFEDRSMI
     VTRFADRLRA ASIVEFARAD MAPDPRKWAR IRGHVAALGL SLAPPLEPWM GARPTLPDYL
     PAIGRRGAVA YAFGHQHLGL TLAATSGEAL AALLHDAPPP FDLSPFTLDR FR
//