ID A0A0Q9L8T5_9MICC Unreviewed; 446 AA.
AC A0A0Q9L8T5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glycine oxidase {ECO:0000313|EMBL:KRE50273.1};
GN ORFNames=ASG92_08185 {ECO:0000313|EMBL:KRE50273.1};
OS Arthrobacter sp. Soil736.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736395 {ECO:0000313|EMBL:KRE50273.1, ECO:0000313|Proteomes:UP000051775};
RN [1] {ECO:0000313|Proteomes:UP000051775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil736 {ECO:0000313|Proteomes:UP000051775};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE50273.1, ECO:0000313|Proteomes:UP000051775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil736 {ECO:0000313|EMBL:KRE50273.1,
RC ECO:0000313|Proteomes:UP000051775};
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:KRE50273.1}.
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DR EMBL; LMSB01000045; KRE50273.1; -; Genomic_DNA.
DR RefSeq; WP_056633018.1; NZ_LMSB01000045.1.
DR AlphaFoldDB; A0A0Q9L8T5; -.
DR STRING; 1736395.ASG92_08185; -.
DR OrthoDB; 3214401at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000051775; 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 18..402
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 337..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 45939 MW; 82B2618515045FCC CRC64;
MNPGSGGNTS ATPTLHADVA VIGGGVVGHG IAWEARRSGR SVVLIDESPG TGASWAAAGM
LAPVSELHYQ EEGLLELMLE SSARWPAFAA ALADGGRDTG YLPTPTLAVG ADPADRRALM
DLREVQRASG LVVEPLTIRE ARSREPLLSP GISCALDIPA DHQVDPRRLV ESLAAALAEH
TPGSGTAVAG AWKGYAVREH ATGLLWDSAG VCGVRLTGGG TVRAAETVVA NGLAAGSLDG
LPEGLRLPLR PVYGDILRLR IPERLRPLLT ATVRGMVRGV PVYLVPRRDG TVVIGATQRE
DDLSGPSAGG VYQLLRDAQS LVPAVAELEL LESTARARPG TPDNAPLLGR VPSGPVPSGR
GSGPAVAGAA VPGPAVARTS VAGLIIATGF FRHGVLLTPA ASVICRELMD GVEDGRWDAF
RPGRFSPELS GSSPSGTATF IRPSHI
//
