ID B7NCW3_ECOLU Unreviewed; 499 AA.
AC B7NCW3;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Glycolate oxidase subunit, FAD-linked {ECO:0000313|EMBL:CAR14613.1};
GN Name=glcD {ECO:0000313|EMBL:CAR14613.1};
GN OrderedLocusNames=ECUMN_3455 {ECO:0000313|EMBL:CAR14613.1};
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056 {ECO:0000313|EMBL:CAR14613.1, ECO:0000313|Proteomes:UP000007097};
RN [1] {ECO:0000313|Proteomes:UP000007097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC {ECO:0000313|Proteomes:UP000007097};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CU928163; CAR14613.1; -; Genomic_DNA.
DR RefSeq; WP_000026117.1; NC_011751.1.
DR RefSeq; YP_002414120.1; NC_011751.1.
DR AlphaFoldDB; B7NCW3; -.
DR STRING; 585056.ECUMN_3455; -.
DR GeneID; 75205189; -.
DR KEGG; eum:ECUMN_3455; -.
DR PATRIC; fig|585056.7.peg.3632; -.
DR HOGENOM; CLU_017779_9_2_6; -.
DR Proteomes; UP000007097; Chromosome.
DR GO; GO:0009339; C:glycolate oxidase complex; IEA:InterPro.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 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; IPR004490; GlcD.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR00387; glcD; 1.
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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT DOMAIN 52..230
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 499 AA; 53812 MW; 2D850E109DD1BA55 CRC64;
MSILYEERLD GALPDVDRTS VLMALREHVP GLEILHTDEE IIPYECDGLS AYRTRPLLVV
LPKQMEQVTA ILAVCHRLRV PVVTRGAGTG LSGGALPLEK GVLLVMARFK EILDINPVGR
RARVQPGVRN LAISQAVAPH NLYYAPDPSS QIACSIGGNV AENAGGVHCL KYGLTVHNLL
KIEVQTLDGE ALTLGSDALD SPGFDLLALF TGSEGMLGVT TEVTVKLLPK PPVARVLLAS
FDSVEKAGLA VGDIIANGII PGGLEMMDNL SIRAAEDFIH AGYPVDAEAI LLCELDGVES
DVQEDCERVN DILLKAGATD VRLAQDEAER VRFWAGRKNA FPAVGRISPD YYCMDGTIPR
RALPGVLEGI ARLSQQYDLR VANVFHAGDG NMHPLILFDA NEPGEFARAE ELGGKILELC
VEVGGSISGE HGIGREKINQ MCAQFNSDEI TTFHAVKAAF DPDGLLNPGK NIPTLHRCAE
FGAMHVHHGH LPFPELERF
//