ID A6GRB5_9BURK Unreviewed; 496 AA.
AC A6GRB5;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=Glycolate oxidase subunit {ECO:0000313|EMBL:EDM83388.1};
GN ORFNames=LMED105_07298 {ECO:0000313|EMBL:EDM83388.1};
OS Limnobacter sp. MED105.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Limnobacter.
OX NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM83388.1, ECO:0000313|Proteomes:UP000010322};
RN [1] {ECO:0000313|EMBL:EDM83388.1, ECO:0000313|Proteomes:UP000010322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED105 {ECO:0000313|EMBL:EDM83388.1,
RC ECO:0000313|Proteomes:UP000010322};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDM83388.1}.
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DR EMBL; ABCT01000008; EDM83388.1; -; Genomic_DNA.
DR RefSeq; WP_008250580.1; NZ_ABCT01000008.1.
DR AlphaFoldDB; A6GRB5; -.
DR STRING; 391597.LMED105_07298; -.
DR OrthoDB; 8522822at2; -.
DR Proteomes; UP000010322; 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:UP000010322}.
FT DOMAIN 49..227
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 496 AA; 53214 MW; 828620546AFADC57 CRC64;
MNAPTEDFVL NAAQRAEVIT GLNQILPAHA VLHEVEDTKP YECDGLSLFR QLPMVVALPE
TEEQVIQILK LANRLNVPVV ARGAGTGLSG GAQPHKHGIL LGMAKFNKIL KVDVQSRSAV
VQPGVRNLAI SEAVAQHQLY YAPDPSSQIA CTIGGNVAEN SGGVHCLKYG LTVHNVLKVR
AITIEGEIVE FGSEAPDAPG LELMNLVIGS EGMLAVVTEV TVKLVPKPAL AQVIMASFDD
VANAGNAVAA VIAAGIIPAG LEMMDKRASQ MVEPFVKAGY DTEAEAILLL ESDGTPEEVA
EEIAEMTRVL NGCGATAIKV SQSEAERLKF WAGRKNAFPA AGRVSPDYYC MDGTIPRRRL
ADVLNAITEM EKKYDMRCAN VFHAGDGNLH PLILFDANKP EEIKRAEDFG AEILELCVEV
GGTVTGEHGV GIEKINQMCV QFSRAELDAF FAVKKAFDEP GLLNPGKAIP TLHRCAEYGR
MHVHGGQVPF ADLPRF
//
