ID A0A0Q8E2Z6_9ACTN Unreviewed; 458 AA.
AC A0A0Q8E2Z6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:KRA38957.1};
GN ORFNames=ASD81_10355 {ECO:0000313|EMBL:KRA38957.1};
OS Nocardioides sp. Root614.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736571 {ECO:0000313|EMBL:KRA38957.1, ECO:0000313|Proteomes:UP000051699};
RN [1] {ECO:0000313|EMBL:KRA38957.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA38957.1,
RC ECO:0000313|Proteomes:UP000051699};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA38957.1, ECO:0000313|Proteomes:UP000051699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root614 {ECO:0000313|EMBL:KRA38957.1,
RC ECO:0000313|Proteomes:UP000051699};
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:KRA38957.1}.
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; LMGV01000001; KRA38957.1; -; Genomic_DNA.
DR RefSeq; WP_056709827.1; NZ_LMGV01000001.1.
DR AlphaFoldDB; A0A0Q8E2Z6; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000051699; 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:UP000051699}.
FT DOMAIN 40..219
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 458 AA; 47761 MW; 0C1E09C836716AF2 CRC64;
MTPSEQGGLR TLEELLPSEI VVTDPDVIAS YARDQSRFTD SCLPLAVLMP RTTDEVSRSL
KVLHELGIPT VARGAGSGLS GAANASPGCV VMSLHRMNEI LEIDVEDRLA VVQPGVVTAT
LRAAVSAAGL FYPPDPGSVE MCTIGGNAST NAGGMCCVKY GVTGDFVIGL EVVLADGRVM
RTGRRTVKGV AGYDLTRLFV GSEGTLGVIT EITVRLVPGP PAAQTLVASF ASLSHAGAAV
AGVTRAGLTP SLMEILDRTT VQAVDEMSHM GLGRDVAALL LIQSDDQDAT GLLSLVEDIC
RQCGAVDVAR SSDPTEAALL LEARRLALPA LERLGDWLLD DVAVPRSRIV ELIGAIEEIG
QQLGIVIGVF GHAGDGNLHP TVIFDDTDPA SRAVAVAAFD AITQKALDLG GTITGEHGTG
RLKRGWLARE LDPTSRSVQT AIKAALDPDN LLNPAVAW
//