ID B7MA37_ECO45 Unreviewed; 499 AA.
AC B7MA37;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Glycolate oxidase subunit, FAD-linked {ECO:0000313|EMBL:CAR04586.1};
GN Name=glcD {ECO:0000313|EMBL:CAR04586.1};
GN OrderedLocusNames=ECS88_3354 {ECO:0000313|EMBL:CAR04586.1};
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR04586.1, ECO:0000313|Proteomes:UP000000747};
RN [1] {ECO:0000313|Proteomes:UP000000747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
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; CU928161; CAR04586.1; -; Genomic_DNA.
DR RefSeq; WP_000026154.1; NC_011742.1.
DR AlphaFoldDB; B7MA37; -.
DR KEGG; ecz:ECS88_3354; -.
DR HOGENOM; CLU_017779_9_2_6; -.
DR Proteomes; UP000000747; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000747}.
FT DOMAIN 52..230
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 499 AA; 53856 MW; 2239AA62E864A573 CRC64;
MSILYEERLD GALPEVDRTS VLMALREHVP GLEILHTDEE IIPYECDGLS AYRTRPLLVV
LPKQMEQVTA ILAVCHRLRV PVVTRGAGTG LSGGALPLEK GVLLVMARFK EILDINPIGR
RARVQPGVRN LAISQAVAPH NLYYAPDPSS QIACSIGGNV AENAGGVHCL KYGLTVHNLL
KIEVQMLDGE ALTLGSDALD SPGFDLLALF TGSEGMLGVT TEVTVKLLPK PPVARVLLAS
FDSVEKAGLA VGDIIANGII PGGLEMMDNL SIRAAEDFIH AGYPVDAEAI LLCELDGVES
DVQEDCERVN DILLNAGATD VRLAQDEAER VRFWAGRKNA FPAVGRISPD YYCMDGTIPR
RALPGVLEGI ARLSQQYDLR VANVFHAGDG NMHPLILFDA NEPGEFARAE ELGGKILELC
VEVGGSISGE HGIGREKINQ MCAQFNSDEI TTFHAVKAAF DPDGLLNPGK NIPTLHRCAE
FGAMHVHHGH LPFPELERF
//