ID J1ECZ3_9BURK Unreviewed; 410 AA.
AC J1ECZ3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Glycine/D-amino acid oxidase, deaminating {ECO:0000313|EMBL:EJE50119.1};
GN ORFNames=PMI14_05324 {ECO:0000313|EMBL:EJE50119.1};
OS Acidovorax sp. CF316.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE50119.1, ECO:0000313|Proteomes:UP000004811};
RN [1] {ECO:0000313|EMBL:EJE50119.1, ECO:0000313|Proteomes:UP000004811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF316 {ECO:0000313|EMBL:EJE50119.1,
RC ECO:0000313|Proteomes:UP000004811};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJE50119.1}.
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; AKJX01000200; EJE50119.1; -; Genomic_DNA.
DR RefSeq; WP_007858438.1; NZ_AKJX01000200.1.
DR AlphaFoldDB; J1ECZ3; -.
DR PATRIC; fig|1144317.3.peg.4870; -.
DR Proteomes; UP000004811; 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; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000004811}.
FT DOMAIN 4..391
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 410 AA; 43708 MW; C715CCB3FE273E0C CRC64;
METIVLGAGM VGVSTALALQ QRGHAVTLVD RKAPGQETSY GNAGIIQREA VQPYAFPRNI
ATLARIATGL SNDAHYHWGA VLRLAPQLLG YWAASAPGRY APIAQAYSRL IAHCLTEHGG
WIEAAGAADL VHRQGWMQLY RTAPVFDAAA TQARATAAAH GLACQVLDTA ALAAAQPVLQ
MPLAGAVHWQ DPWTVRDPGE LVARYARLFV QRGGHLATGD AMAVRQEGSG WAVQVDSGSI
SAQHAVIALG PWAGALTTRL GYRLPLFSKR GYHRHFAGGP SLNMPALDIE RGVMLAPMAR
GLRLTTGAEF ALLDAPATPV QLRRAEQSTR ELLPLGEPVE ATPWLGARPC TADMLPVLGK
APRHTGLWFN FGHAHQGFTL GPVTGRLVAE LISGEAPFVD PAPYLAQRFL
//
