ID A0A0P7VU60_9RHOB Unreviewed; 347 AA.
AC A0A0P7VU60;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glycine/D-amino acid oxidases (Deaminating) {ECO:0000313|EMBL:KPP90603.1};
GN ORFNames=HLUCCA08_14735 {ECO:0000313|EMBL:KPP90603.1};
OS Rhodobacteraceae bacterium HLUCCA08.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666913 {ECO:0000313|EMBL:KPP90603.1, ECO:0000313|Proteomes:UP000050293};
RN [1] {ECO:0000313|Proteomes:UP000050293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KPP90603.1, ECO:0000313|Proteomes:UP000050293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA08 {ECO:0000313|EMBL:KPP90603.1};
RX PubMed=26497460; DOI=10.1128/AEM.02274-15;
RA Nelson W.C., Maezato Y., Wu Y.W., Romine M.F., Lindemann S.R.;
RT "Identification and Resolution of Microdiversity through Metagenomic
RT Sequencing of Parallel Consortia.";
RL Appl. Environ. Microbiol. 82:255-267(2016).
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:KPP90603.1}.
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DR EMBL; LJSF01000010; KPP90603.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7VU60; -.
DR STRING; 1666913.HLUCCA08_14735; -.
DR PATRIC; fig|1666913.4.peg.575; -.
DR Proteomes; UP000050293; 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; 2.
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; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR13847:SF293; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN MNMC; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
FT DOMAIN 5..328
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 347 AA; 35730 MW; 43DB533B389A3F38 CRC64;
MTSPDVTVRG AGAFGLSVAW ACAARGARVR VVDPQGVGAG ASGGVVGALA PHAPEHWTEA
KAFQLDSLLM ADAWWAAVAA AGGRSPGYGR TGRLQPIADD AALERARARA ENAAGLWRGQ
AEWRIVDRTD IGDFAPDSPS DMWIFDTLSA RLSPLAACRA LAAAITARGG EVVAEAPDAG
AVVWATGWQG LVAMSAGRDR RVGTGIKGQA ALLALAARDA PQLYAPGLHV VPHADGTVAV
GSTTERDVDA PAATDDQLDA VIARARALCP ALRDAPVTRR WAGVRPRSRT RAPMLGAHPL
RPGQFVANGG FKIGFGVAPL AGEAMADLVL EGDGRRIPDS FDPAASL
//