ID A0A085FKK4_9BURK Unreviewed; 348 AA.
AC A0A085FKK4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Glycolate oxidase subunit GlcE {ECO:0000313|EMBL:KFC71999.1};
GN Name=glcE1 {ECO:0000313|EMBL:KFC71999.1};
GN ORFNames=FG94_02032 {ECO:0000313|EMBL:KFC71999.1};
OS Massilia sp. LC238.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC71999.1, ECO:0000313|Proteomes:UP000028601};
RN [1] {ECO:0000313|EMBL:KFC71999.1, ECO:0000313|Proteomes:UP000028601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC238 {ECO:0000313|EMBL:KFC71999.1,
RC ECO:0000313|Proteomes:UP000028601};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (JUN-2014) 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:KFC71999.1}.
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; JNNN01000038; KFC71999.1; -; Genomic_DNA.
DR RefSeq; WP_036210617.1; NZ_JNNN01000038.1.
DR AlphaFoldDB; A0A085FKK4; -.
DR STRING; 1502852.FG94_02032; -.
DR PATRIC; fig|1502852.3.peg.1974; -.
DR eggNOG; COG0277; Bacteria.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000028601; 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;
FT DOMAIN 1..169
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 348 AA; 37540 MW; 397D940A9B40B8B6 CRC64;
MQSIEQFQQR VRAAAADKQS LRIRGGGSKD WYGQRLEGEI LDTRGYTGIV DYEPTELVIT
ARCGTPLAEI EAVLAERNQM LAFEPPHFGD GATLGGAIAA GLAGPRRATS GGVRDFVLGA
KLLDGKGDVL TFGGQVMKNV AGYDVSRMLA GSLGTLGLLL EVSVKVLPKP FAETTLCLEL
SEVEAIRKLN EWGGQPLPLS ASCWHNGSLW LRLSGAQAAV DAAVRLIGGE TMPNSACFWE
ELREQRLPFF GGEEALWRLS LPSTTDTLKL GGVQLIEWGG AQRWLRTDRD AATIRATVSA
SGGHTTLFRG GDKSVGVFQP LQPAVARIHE RLKNSFDPAH IFNPGRLY
//
