ID A0A0Q6ZBS5_9BRAD Unreviewed; 497 AA.
AC A0A0Q6ZBS5;
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=Glycolate oxidase subunit GlcD {ECO:0000313|EMBL:KQW21544.1};
GN ORFNames=ASC80_13685 {ECO:0000313|EMBL:KQW21544.1};
OS Afipia sp. Root123D2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW21544.1, ECO:0000313|Proteomes:UP000051348};
RN [1] {ECO:0000313|EMBL:KQW21544.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW21544.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW21544.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW21544.1,
RC ECO:0000313|Proteomes:UP000051348};
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:KQW21544.1}.
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DR EMBL; LMDP01000002; KQW21544.1; -; Genomic_DNA.
DR RefSeq; WP_056298962.1; NZ_LMDP01000002.1.
DR AlphaFoldDB; A0A0Q6ZBS5; -.
DR STRING; 1736436.ASC80_13685; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000051348; 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:SF1; 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:UP000051348}.
FT DOMAIN 50..228
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 497 AA; 53148 MW; 6C5ABAB0509D5CD4 CRC64;
MSIMMPAADE AILGRRDEIV AALRNIVPGE GVIANPSEML PYESDALTAY RQLPMVVVLP
DTTEQVSQVL KYCHANGIKV VPRGSGTSLS GGSLPLKDGV LLGLSKFKRV REIDFENRVA
VVEPGVTNLA ISQAVAHAGF YYAPDPSSQI ACSIGGNIAE NSGGVHSLKY GMTTNNVLGC
EFVLITGEIL RIGSKAPEND GYDLMGVITG SEGLLGVVTE VTVRILQKPE TARALMVGFA
EVEAAGQCVA DIIGAGIIPG GMEMMDRDAI HAAEAFVHAG YPLDVEALLI IELDGPKVEV
DELIARVEKI ALGCGSTTCQ ISNSEQERLL FWAGRKAAFP AVGRLSPDYL CMDGTIPRGK
LPEALAGIRD LSKKYGLRCA NVFHAGDGNL HPLILYDANI ADEMQRAEDF GADILRLCVK
LGGVLTGEHG VGVEKRDLMP EMFTEIDLAQ QQRLKCAFDS GGLLNPGKVF PTLHRCAELG
RVHVHHGKLA FPDIPRF
//
