ID A0A0C1JQ98_9RHOB Unreviewed; 478 AA.
AC A0A0C1JQ98;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Glycolate oxidase subunit GlcD {ECO:0000313|EMBL:KIC46267.1};
GN ORFNames=RA28_00125 {ECO:0000313|EMBL:KIC46267.1};
OS Ruegeria sp. ANG-S4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1577904 {ECO:0000313|EMBL:KIC46267.1, ECO:0000313|Proteomes:UP000031326};
RN [1] {ECO:0000313|Proteomes:UP000031326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S4 {ECO:0000313|Proteomes:UP000031326};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(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:KIC46267.1}.
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; JWLK01000001; KIC46267.1; -; Genomic_DNA.
DR RefSeq; WP_039522338.1; NZ_JWLK01000001.1.
DR AlphaFoldDB; A0A0C1JQ98; -.
DR STRING; 1577904.RA28_00125; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000031326; 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:UP000031326}.
FT DOMAIN 48..226
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 478 AA; 51051 MW; 58CD9FC4913B284D CRC64;
MEMPRPNPDV LARKQSVMSR LLQVLPADAV IHDPAETRAY ECDALTAYRC PPMLAVLPAS
TQEVSDVLRI CREEGVPVVP RGSGTSLAGG ALPTADCVIL GVARMTEVLE TDYDNRFIRV
QTGRTNLSVT GAVEEEDFFY APDPSSQLAC AIAGNIAMNS GGAHCLKYGV TTNNLLGVTM
VLMDGTVVEV GGAHLDSGGL DLLGVICGSE GQLGVVTEAT LRILRKPEGA RPVLLGFDDT
AVAGRCVSDI IKSGILPVAI EFMDALCIQV CENFAHAGYP DCAALLIVEV EGSEAEIDHQ
LSKIIEIAKR HKPVEIRESQ SAEESAKIWL GRKSAFGAMG QVNDYMCLDG TIPVSSLPDV
LRRIGELSED YGLPVGNVFH AGDGNMHPLI LFDANKPGDL EKCEAFGADI LKLCVDAGGC
LTGEHGVGIE KRDLMTHQYA PQDLEAQMAI KDVFDPDWLL NPAKVFPLDV SEARRAAA
//
