ID A0A0Q6R726_9MICO Unreviewed; 453 AA.
AC A0A0Q6R726;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KQV25179.1};
GN ORFNames=ASC54_12070 {ECO:0000313|EMBL:KQV25179.1};
OS Yonghaparkia sp. Root332.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microcella.
OX NCBI_TaxID=1736516 {ECO:0000313|EMBL:KQV25179.1, ECO:0000313|Proteomes:UP000051768};
RN [1] {ECO:0000313|EMBL:KQV25179.1, ECO:0000313|Proteomes:UP000051768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root332 {ECO:0000313|EMBL:KQV25179.1,
RC ECO:0000313|Proteomes:UP000051768};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV25179.1, ECO:0000313|Proteomes:UP000051768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root332 {ECO:0000313|EMBL:KQV25179.1,
RC ECO:0000313|Proteomes:UP000051768};
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:KQV25179.1}.
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DR EMBL; LMCX01000002; KQV25179.1; -; Genomic_DNA.
DR RefSeq; WP_055899264.1; NZ_LMCX01000002.1.
DR AlphaFoldDB; A0A0Q6R726; -.
DR STRING; 1736516.ASC54_12070; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000051768; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051768}.
FT DOMAIN 37..216
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 453 AA; 46635 MW; E652083552142546 CRC64;
MSGHPALTAL RDALGDALST EPAALEAARG DYSGLRRNGT PLAVVHARTI ADVQAALRIA
TEHRLPVVPR GAGTGLTGGA MGGEGELVLS TARMTRVIEV SPADQLAVVE PGVINAELNA
ALEPTGLFFA PDPASRAIST IGGNIATNAG GLLCAKYGVT REAVLGLKVV LADGTLLELG
HRTVKGVTGL DLTALVIGSE GTLGVVVEAT VRLMPLPAGS PATIGAYFPS VVDAAAASAA
ITAAHLRPAV MELIDEVALA RILAHLGLPE RAPGSAYLLV QTDGSAAIAE AEEALAIIRA
HDGAAALTAD PDEGERMLAV RRAFHPAMAA SANVLIEDVA VPRSALPEML AAIREIGARH
DLEIPTVAHA GDGNLHPNFL FAGDEVPPRV WEAAGELFRT AMSLGGTLTG EHGVGTLKRQ
WLEEELGAPQ LDLQRRIKAV FDPLGIMNPG KVF
//
