ID B1XXJ7_LEPCP Unreviewed; 455 AA.
AC B1XXJ7;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=D-amino-acid dehydrogenase {ECO:0000313|EMBL:ACB35117.1};
DE EC=1.4.99.6 {ECO:0000313|EMBL:ACB35117.1};
GN OrderedLocusNames=Lcho_2852 {ECO:0000313|EMBL:ACB35117.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB35117.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB35117.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) 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 ---------------------------------------------------------------------------
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; CP001013; ACB35117.1; -; Genomic_DNA.
DR RefSeq; WP_012347871.1; NC_010524.1.
DR AlphaFoldDB; B1XXJ7; -.
DR STRING; 395495.Lcho_2852; -.
DR KEGG; lch:Lcho_2852; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_9_2_4; -.
DR OrthoDB; 18526at2; -.
DR Proteomes; UP000001693; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:ACB35117.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001693}.
FT DOMAIN 3..433
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 237..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 49061 MW; E95550323EDFEC65 CRC64;
MRVGVVGAGI AGVTTAFELA EAGHEVTVYE RCDAVAEAAS FAHAGLLTAG LVSPAAAPGL
RRWLLRGLRH HESALRWRPG LDPAHYQWLW QWWRASSSGH AGDVRAMTEL AVISLQRLDQ
LTRDLGLSHE RSRGVLVLLR DSRELAPTHR HAGMLRELGW AVNELTPQAC LEIEPHLGRS
RLAGGLHLPD DGVGNCRQMT QQLRDHAERR QGVQFTFGTE VGAIRTEGRQ ITLQLRARER
DAATPSRPGP VLRSRASAAH PPDTAEADFV PTQPLDRDRQ ATHDAVVLCS GADTTLVHRH
AQALPIQPVW GHAATFRIHP DGQALQSAVV DASAGVTLSR LGPRLRVTGG FELGGSPGPA
GEAALSPLYA ALDRWFPHAT ERRQAQIWRG ARPMLPHGPP VIGPSATPGV WLNLGHGAHG
WTLACGSARL LAEQISGRPC STDPAPFAAS RWAHP
//
