ID   A0A0G1V8A4_9BACT        Unreviewed;       553 AA.
AC   A0A0G1V8A4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KKW02713.1};
GN   ORFNames=UY36_C0003G0005 {ECO:0000313|EMBL:KKW02713.1};
OS   Parcubacteria group bacterium GW2011_GWA1_49_11.
OC   Bacteria.
OX   NCBI_TaxID=1618796 {ECO:0000313|EMBL:KKW02713.1, ECO:0000313|Proteomes:UP000033954};
RN   [1] {ECO:0000313|EMBL:KKW02713.1, ECO:0000313|Proteomes:UP000033954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(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:KKW02713.1}.
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DR   EMBL; LCPS01000003; KKW02713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1V8A4; -.
DR   Proteomes; UP000033954; 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   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; IPR016167; FAD-bd_PCMH_sub1.
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; 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;
FT   DOMAIN          30..267
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   553 AA;  62227 MW;  39D6A51838745253 CRC64;
     MIEDLRGIVK GEISIEEEEL KNKSRDASIF EVKPEAVVYP KDVEDLKNIV SWASECKAEN
     PNLSLTARSA GTDMTGGPLN DSVILDFTRY FNRVGEVTAI PPDGGIAVVE PGVYYRDFEK
     ETLAKNLLMP SYPASREICT VGGMAANNSG GEKSLRFGQT VRYVEELAVV LSDGNEYTLH
     GLDQNELAQK ISQQDFEGEV YRRMRGLIED NYDVILSAKP DVTKNSAGYL LWDVWPNRET
     FNLAKLFVGS QGTLGLITKI KFRLIRPKKY SKLLVIFLND LAPLGELVKE VVKFKPESFE
     AFDDQALKLA VKFLPDIMKN IKTGAFSLAL KFLPELGMMI MGGVPELVLI AEFTGETESE
     ADDKLKMAEP AVKKKFPSLK THITRSLEEA EKYWIMRRES FNLLRHHVQG KHTAPFIDDV
     IVHVDQLPEF LPRLKDLIGQ YPGLTYTVAG HAGDANFHVI PLMDFSDEAN QRIIPELSEK
     VYDLVVSMKG SITAEHNDGL IRTPYLEKMY GPKICELFRQ TKEIFDPLNI FNPRKKVLPD
     KDFARTHIAK TNG
//