ID A0A0Q8CTS2_9MICO Unreviewed; 469 AA.
AC A0A0Q8CTS2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KRA12654.1};
GN ORFNames=ASD61_02150 {ECO:0000313|EMBL:KRA12654.1};
OS Leifsonia sp. Root60.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736567 {ECO:0000313|EMBL:KRA12654.1, ECO:0000313|Proteomes:UP000051073};
RN [1] {ECO:0000313|EMBL:KRA12654.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA12654.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA12654.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA12654.1,
RC ECO:0000313|Proteomes:UP000051073};
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:KRA12654.1}.
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DR EMBL; LMGR01000001; KRA12654.1; -; Genomic_DNA.
DR RefSeq; WP_055822662.1; NZ_LMGR01000001.1.
DR AlphaFoldDB; A0A0Q8CTS2; -.
DR STRING; 1736567.ASD61_02150; -.
DR Proteomes; UP000051073; 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:UP000051073}.
FT DOMAIN 41..220
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 469 AA; 47958 MW; 63C45DD8125577C2 CRC64;
MSTIVEADVV AAVSAVVRED QVLTDAASLA AYSHDDAEWA AYERPLAVVL AESTDDVAAV
VAWCATNGVA VVARGSGTGL SGGANAVADS IVLSLERMTT VLEIDTAERY VIAQAGVIND
SLRASVAAHG LWYPPDPASS AISTIGGNAA TNAGGICCVK YGVTRDYVLG MTVVLADGAV
VQLGRRTAKG VAGYDLTALM VGSEGTLGII TELTLKLLPL AGREERAVVG YFPSLHAAGV
AVAGIASAGI IPAALELIDS TCLRAVDDWQ QWGLPCDVEA LLLAKIDDAG ASGDAIADRV
ADAMTTANGV SVERASEQDD VDRLFLARRL AYPALERLGP VLTEDVCVPR IAVPAMLTRI
QAIAAASDVV IANIAHAGDG NLHPLIIAPD GDDAAKARAK VAFDGIIAEC LALGGTVTGE
HGVGLLKLPG LADELGDRVI EMHRAIKLAL DPLNTLNPGK AFPAAAATP
//
