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Database: UniProt
Entry: A0A0Q6FGC5_9ACTN
LinkDB: A0A0Q6FGC5_9ACTN
Original site: A0A0Q6FGC5_9ACTN 
ID   A0A0Q6FGC5_9ACTN        Unreviewed;       380 AA.
AC   A0A0Q6FGC5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Sarcosine oxidase {ECO:0000313|EMBL:KQT93549.1};
GN   ORFNames=ASG49_00615 {ECO:0000313|EMBL:KQT93549.1};
OS   Marmoricola sp. Leaf446.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Marmoricola.
OX   NCBI_TaxID=1736379 {ECO:0000313|EMBL:KQT93549.1, ECO:0000313|Proteomes:UP000051542};
RN   [1] {ECO:0000313|EMBL:KQT93549.1, ECO:0000313|Proteomes:UP000051542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf446 {ECO:0000313|EMBL:KQT93549.1,
RC   ECO:0000313|Proteomes:UP000051542};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT93549.1, ECO:0000313|Proteomes:UP000051542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf446 {ECO:0000313|EMBL:KQT93549.1,
RC   ECO:0000313|Proteomes:UP000051542};
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KQT93549.1}.
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DR   EMBL; LMRF01000001; KQT93549.1; -; Genomic_DNA.
DR   RefSeq; WP_056535734.1; NZ_LMRF01000001.1.
DR   AlphaFoldDB; A0A0Q6FGC5; -.
DR   STRING; 1736379.ASG49_00615; -.
DR   OrthoDB; 9806452at2; -.
DR   Proteomes; UP000051542; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR045170; MTOX.
DR   PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR   PANTHER; PTHR10961:SF7; PEROXISOMAL SARCOSINE OXIDASE; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051542}.
FT   DOMAIN          9..359
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   380 AA;  40077 MW;  505EB634E09E456F CRC64;
     MTTNGTAAYA VVGAGLVGAA TAWQLAARGH DVVVLERGVP ADPGGSSHGS ARIFRYAYAD
     PFYVDLVRQA RLAWDDLETA HGSELVRPTG ALDHGAERDP AGLARALEAV GVEHELLGAS
     EARARFEGID VDSEVLWHPG AGVIDAERAV HAMLDLARSH GARVLTGWAV QEVAATGSGH
     RVTATDGRGL DAGHVVVAAG GWLPGLLDRL GLPSGFRDAV PHLEVWQEEA FHFPHRDGHD
     PWPTTIHGTG EMLTYSLPGG RDAGHRGQKV AQFCGGRAIG TAEHQDGQVD PAHRERIVEH
     VRRTLPGLVP EPYAETTCLF TSTPTEDFVL DRCEGLTLVS ACSGHGAKFA PLLGAMVADA
     AAATDPDAAR RLVPARFHVG
//
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