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Database: UniProt
Entry: A0A0Q9NHQ9_9MICC
LinkDB: A0A0Q9NHQ9_9MICC
Original site: A0A0Q9NHQ9_9MICC 
ID   A0A0Q9NHQ9_9MICC        Unreviewed;       448 AA.
AC   A0A0Q9NHQ9;
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 oxidase {ECO:0000313|EMBL:KRE74131.1};
GN   ORFNames=ASG77_05125 {ECO:0000313|EMBL:KRE74131.1};
OS   Arthrobacter sp. Soil762.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736401 {ECO:0000313|EMBL:KRE74131.1, ECO:0000313|Proteomes:UP000051715};
RN   [1] {ECO:0000313|Proteomes:UP000051715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil762 {ECO:0000313|Proteomes:UP000051715};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE74131.1, ECO:0000313|Proteomes:UP000051715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil762 {ECO:0000313|EMBL:KRE74131.1,
RC   ECO:0000313|Proteomes:UP000051715};
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   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
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:KRE74131.1}.
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DR   EMBL; LMSG01000012; KRE74131.1; -; Genomic_DNA.
DR   RefSeq; WP_056343947.1; NZ_LMSG01000012.1.
DR   AlphaFoldDB; A0A0Q9NHQ9; -.
DR   OrthoDB; 3214401at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000051715; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012727; Gly_oxidase_ThiO.
DR   NCBIfam; TIGR02352; thiamin_ThiO; 1.
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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
FT   DOMAIN          23..400
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   REGION          414..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  46244 MW;  307C8F465CD1AC8F CRC64;
     MPPAISSPPE PAPASAATAL HADVAVIGGG VIGHAIAWEV RRSGRSVVLI DDAPGNGASW
     AAAGMLAPVS ELHYQEEDLL ELMLASSGLW PAFAADLALA GAGDTGYLTT PTLAIGADAA
     DRRALMDLRA VQQASGLVVE PLTVREARTR ESLLSPAISC ALDIPADHQV DPRRLVACLQ
     EVLAIHEPGA GTAVAGARAG FAVDQRAAAL LWEDGRVIGV KLAHGGTVQA RETIVANGLQ
     AGSLEGLPVG LHLPLRPVYG DILRLAVPRH LRPLLTSTVR GMVHGVPVYI VPRQDGTVVI
     GATQREDALA GSGDAAVSAG GVYQLLRDAQ VLVPAVSELE LLECTARARP ATPDNAPLLG
     RVPVSAPRTG NTANIAGLMV ATGFFRHGVL LAPAAAAICR DLLDGRTDPR WGALSPARFS
     GKHHVAGTQS PDKDISSTKD LDPQKESA
//
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