ID A0A0P4UVW0_9CYAN Unreviewed; 489 AA.
AC A0A0P4UVW0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Glycolate dehydrogenase, subunit GlcD {ECO:0000313|EMBL:GAP95661.1};
DE EC=1.1.99.14 {ECO:0000313|EMBL:GAP95661.1};
GN ORFNames=NIES2104_21850 {ECO:0000313|EMBL:GAP95661.1};
OS Leptolyngbya sp. NIES-2104.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAP95661.1, ECO:0000313|Proteomes:UP000052243};
RN [1] {ECO:0000313|EMBL:GAP95661.1, ECO:0000313|Proteomes:UP000052243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2104 {ECO:0000313|EMBL:GAP95661.1,
RC ECO:0000313|Proteomes:UP000052243};
RX PubMed=26494835; DOI=10.1093/dnares/dsv022;
RA Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H.,
RA Kawachi M.;
RT "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES-2104
RT and the freshwater Leptolyngbya boryana PCC 6306 genomes.";
RL DNA Res. 22:403-412(2015).
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:GAP95661.1}.
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; BBWW01000001; GAP95661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P4UVW0; -.
DR STRING; 1552121.NIES2104_21850; -.
DR InParanoid; A0A0P4UVW0; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000052243; Unassembled WGS sequence.
DR GO; GO:0009339; C:glycolate oxidase complex; IEA:InterPro.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0019154; F:glycolate dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR004490; GlcD.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR00387; glcD; 1.
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 Oxidoreductase {ECO:0000313|EMBL:GAP95661.1}.
FT DOMAIN 44..222
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 489 AA; 52412 MW; AD0DC4ECBDA33289 CRC64;
MTAIVTQPNW QAIAREFEAV VGKSGVVRKR EELLVYECDG LTSYRERPEL VVLPRTTEQV
AAVVKICDRH LVPFVARGSG TGLSGGALPI QNCVLIVTSL MRKILKVDLE NQRVVVQPGV
INSWVTQTVS GAGFYYAPDP SSQIICSIGG NVAENSGGVH CLKYGVTTNH VLGVKIVTPD
GSIVELGGDL PEMPGYDLTG VFVGSEGTLG IATEITLKIL KTPESIRVLL ADFTSVEAAG
ATVSDIISAG IIPGGMEMMD NMSINAVEDV VATGCYPRDA TAILLVEVDG LEVEAEVNSQ
RVAEICRKNG ARNVTVATEA DERLTIWKGR KAAFAAMGKM SPDYYVQDGV IPRTKLEYVL
SEIEALGEKH GYKVANVFHA GDGNLHPLIL YDNAVPGALE QVEELGGEIL KLCVKVGGSI
SGEHGIGADK RCYMPEMFTP ADLDTMQWVR EAFDPKGIAN PTKLFPTPRT CGEAAKASGQ
KTFENVDRF
//
