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}.
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; 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
//