ID E3HEK0_ACHXA Unreviewed; 368 AA.
AC E3HEK0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Glycolate oxidase subunit GlcE {ECO:0000313|EMBL:ADP15245.1};
DE EC=1.1.3.15 {ECO:0000313|EMBL:ADP15245.1};
GN Name=glcE {ECO:0000313|EMBL:ADP15245.1};
GN OrderedLocusNames=AXYL_01912 {ECO:0000313|EMBL:ADP15245.1};
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP15245.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|EMBL:ADP15245.1, ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:ADP15245.1,
RC ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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; CP002287; ADP15245.1; -; Genomic_DNA.
DR RefSeq; WP_013392578.1; NC_014640.1.
DR AlphaFoldDB; E3HEK0; -.
DR STRING; 762376.AXYL_01912; -.
DR KEGG; axy:AXYL_01912; -.
DR PATRIC; fig|762376.5.peg.1910; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_0_0_4; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000006876; Chromosome.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:ADP15245.1}.
FT DOMAIN 1..176
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 368 AA; 38766 MW; 8B0078C53870A0F5 CRC64;
MDFVLSELCD QVMTARAGHK PLFVMGGGSK AFYGNYRPVT PQDGHCLLDM TPYRGIVSYH
PSELVVTVRA GTPLAELEAA LAENGQMLAF EPPHFSVSAT VGGCVAAGLS GPRRMSAGAL
KDFVLGAQLL DSEGRILSFG GEVMKNVAGY DVSRLLAGSH GIFGAILEVS LKVVPRPMQE
ITLALPATQA QALASFALWR GKPLPISATS WSGDDEGAEG QMAVRLSGAP PAVASARQLI
GGAPMAPEAA QAWWRSLREQ THSFFAPGRP LWRLALPPTA AALGLGPTLL EWGGGQRWLS
GEQDAAALRE TAERLGGHAT LFRAGQGRPP ADGVFHPLAP GIASITRRLK QELDPAGLFN
PGRLVLDL
//
