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Database: UniProt
Entry: A0A098TL42_9CYAN
LinkDB: A0A098TL42_9CYAN
Original site: A0A098TL42_9CYAN 
ID   A0A098TL42_9CYAN        Unreviewed;       430 AA.
AC   A0A098TL42;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Glycolate oxidase {ECO:0000313|EMBL:KGF73006.1};
GN   ORFNames=DO97_02870 {ECO:0000313|EMBL:KGF73006.1};
OS   Neosynechococcus sphagnicola sy1.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales;
OC   Neosynechococcaceae; Neosynechococcus.
OX   NCBI_TaxID=1497020 {ECO:0000313|EMBL:KGF73006.1, ECO:0000313|Proteomes:UP000030170};
RN   [1] {ECO:0000313|EMBL:KGF73006.1, ECO:0000313|Proteomes:UP000030170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAUP A 1101 {ECO:0000313|EMBL:KGF73006.1,
RC   ECO:0000313|Proteomes:UP000030170};
RA   Dvorak P., Casamatta D., Hasler P., Poulickova A., Ondrej V., Sanges R.;
RT   "Evolution of Synechococcus.";
RL   Mol. Ecol. 0:0-0(2014).
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:KGF73006.1}.
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DR   EMBL; JJML01000016; KGF73006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A098TL42; -.
DR   STRING; 1497020.DO97_02870; -.
DR   Proteomes; UP000030170; 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   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:UP000030170}.
FT   DOMAIN          29..208
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   430 AA;  45896 MW;  2D964CA12937DCD6 CRC64;
     MDQLGAEAVT TWEDLALTQQ QKFRQAVTPE TQISCVVSPT TLEELGAIMA AAHRHRWRVL
     PCGRGSKIHW GGLAHPIDLV VSTQRLQNLV EHAVGDLTVT VEAGMQLREL QTRLATAGQF
     LPLDPLYPET ATLGGIVATA SAGSLRQRYG GVRDLLLGIS LVRADGQVAK AGGRVVKNVA
     GYDLMKLFTG SFGTLGILSQ LTFRIYALPE ASQTILLTGA SDRLAQGLQT LMTTALTPTA
     LDLLSTAMVA ALGQKPGLGL LIRFQTIAAG VEEQTRRLLQ LAQTLGLQPQ IYQGADEAAL
     WLQLRAMMEA PPLMTGILCK IGVESESAVA VLSQMDTWTG ATVAAHLQVG SGLGLLQLAA
     GTGSPSLLNQ MRSLCQRHRG FLTLLAAPMA LKQQVDIWGY SGNALPLMQG LKAQFDPQQL
     FSPHRFVGGI
//
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