ID A0A0T6ADC9_9DELT Unreviewed; 463 AA.
AC A0A0T6ADC9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Glycolate oxidase subunit D, glycolate oxidase {ECO:0000313|EMBL:KRT73085.1};
DE EC=1.1.3.15 {ECO:0000313|EMBL:KRT73085.1};
GN Name=glcD {ECO:0000313|EMBL:KRT73085.1};
GN ORFNames=XU12_C0012G0040 {ECO:0000313|EMBL:KRT73085.1};
OS Deltaproteobacteria bacterium CSP1-8.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1640514 {ECO:0000313|EMBL:KRT73085.1, ECO:0000313|Proteomes:UP000051991};
RN [1] {ECO:0000313|EMBL:KRT73085.1, ECO:0000313|Proteomes:UP000051991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-8 {ECO:0000313|EMBL:KRT73085.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-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:KRT73085.1}.
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DR EMBL; LDXO01000012; KRT73085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6ADC9; -.
DR STRING; 1640514.XU12_C0012G0040; -.
DR PATRIC; fig|1640514.3.peg.1576; -.
DR Proteomes; UP000051991; Unassembled WGS sequence.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
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:SF3; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR42934; 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 Oxidoreductase {ECO:0000313|EMBL:KRT73085.1}.
FT DOMAIN 34..213
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 463 AA; 49906 MW; C219718FB8BF4715 CRC64;
MDGQPLSALR DLFGERLFTS REQRICYSYD ATGTMSLPDA VAFPVSAEEV RRTVLLANEH
RFPVIPRGAG SGFSGGSVPV QGGLVLSLER MDRILSIDTE NLVAVVEPGV VTETLKEEAR
KRGLFYPPDP ASLKFCTIGG NIAECSGGMC AVKYGVTRDY VMGLEAVLGT GELIRTGVTT
VKGVVGYDLT RLLVGSEGTL GIVTKAILKL IPFPETAATI LAFFRSNHDG SSAVAGIIRE
RITPCAMELM DRTAIDCVRE EADLPVPDDA GCALLIEVDG PRESVSTEAD RVEQACRQYG
AIEVGRAGDA KGRERLWTLR RSISPALRKV NPVKINEDIV VPRSRLPEMM AFLADVASRR
NLKIVNFGHA GDGNVHVNVM ISGTDEEERR RADEAVSEIF GKTVALGGTI SGEHGIGISK
APFLEMEVGP LGVSVMKRLK GCFDPNGILN PGKIFMEEQM AQR
//
