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Database: UniProt
Entry: W9T8I7_9PSED
LinkDB: W9T8I7_9PSED
Original site: W9T8I7_9PSED 
ID   W9T8I7_9PSED            Unreviewed;       353 AA.
AC   W9T8I7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Glycolate oxidase FAD binding subunit {ECO:0000313|EMBL:EXF43681.1};
GN   Name=glcE {ECO:0000313|EMBL:EXF43681.1};
GN   ORFNames=BAY1663_03897 {ECO:0000313|EMBL:EXF43681.1};
OS   Pseudomonas sp. BAY1663.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF43681.1, ECO:0000313|Proteomes:UP000019475};
RN   [1] {ECO:0000313|EMBL:EXF43681.1, ECO:0000313|Proteomes:UP000019475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAY1663 {ECO:0000313|EMBL:EXF43681.1,
RC   ECO:0000313|Proteomes:UP000019475};
RA   Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT   "Genome sequencing of Pseudomonas sp. BAY1663.";
RL   Submitted (DEC-2013) 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:EXF43681.1}.
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DR   EMBL; AZSV01000070; EXF43681.1; -; Genomic_DNA.
DR   RefSeq; WP_037043057.1; NZ_AZSV01000070.1.
DR   AlphaFoldDB; W9T8I7; -.
DR   STRING; 1439940.BAY1663_03897; -.
DR   PATRIC; fig|1439940.3.peg.3846; -.
DR   eggNOG; COG0277; Bacteria.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000019475; 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   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; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 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:UP000019475}.
FT   DOMAIN          1..174
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   353 AA;  37902 MW;  EC38C5DFB6DC151B CRC64;
     MSVFANDASA QLLDQVNQAL AAKTPLRIQG GGSKAFLGRP VEGQLLDVRE HRGIVSYDPT
     ELVITVRAGT PLAELEAVLD EAGQMLPCEP PHFGPDATVG GMIAAGLSGP RRPWSGSVRD
     FVLGSRIITG QGKHLRFGGE VMKNVAGYDL SRLMAGSFGC LGVLTEVSLK VLPKPRLCSS
     LRLEIDQERA LLELAEWGQQ PIPISAASHD GQALYLRLEG GEGSVRAACG RIGCAELDSD
     YWNALREQRL AFFADARPLW RLSLPNNTPV LGLPGEQLLD WAGAQRWLKS DADAETIRAI
     AHEVGGHATC FSAGATASPF QPLPAPLLRY HQQLKAALDP QGIFNPGRMY SEV
//
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