ID   GLCD_ECOL6              Reviewed;         499 AA.
AC   P0AEQ0; P52075;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Glycolate oxidase subunit GlcD;
DE            EC=1.1.99.14 {ECO:0000250|UniProtKB:P0AEP9};
DE   AltName: Full=Glycolate dehydrogenase subunit GlcD;
GN   Name=glcD; OrderedLocusNames=c3709;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Component of a complex that catalyzes the oxidation of
CC       glycolate to glyoxylate. Is required for E.coli to grow on glycolate as
CC       a sole source of carbon. Is also able to oxidize D-lactate ((R)-
CC       lactate) with a similar rate. Does not link directly to O(2), and 2,6-
CC       dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as
CC       artificial electron acceptors in vitro, but the physiological molecule
CC       that functions as primary electron acceptor during glycolate oxidation
CC       is unknown. {ECO:0000250|UniProtKB:P0AEP9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + glycolate = AH2 + glyoxylate; Xref=Rhea:RHEA:21264,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:36655; EC=1.1.99.14;
CC         Evidence={ECO:0000250|UniProtKB:P0AEP9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21265;
CC         Evidence={ECO:0000250|UniProtKB:P0AEP9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lactate + A = AH2 + pyruvate; Xref=Rhea:RHEA:15089,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:16004,
CC         ChEBI:CHEBI:17499; Evidence={ECO:0000250|UniProtKB:P0AEP9};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- SUBUNIT: The glycolate oxidase likely consists of three subunits, GlcD,
CC       GlcE and GlcF. {ECO:0000250|UniProtKB:P0AEP9}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0AEP9}. Note=Glycolate oxidoreductase activity
CC       was shown to be firmly associated with the cytoplasmic membranes.
CC       {ECO:0000250|UniProtKB:P0AEP9}.
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN82153.1; -; Genomic_DNA.
DR   RefSeq; WP_000026117.1; NC_004431.1.
DR   AlphaFoldDB; P0AEQ0; -.
DR   STRING; 199310.c3709; -.
DR   EnsemblBacteria; AAN82153; AAN82153; c3709.
DR   GeneID; 66673131; -.
DR   KEGG; ecc:c3709; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_9_2_6; -.
DR   OMA; TPRTCGE; -.
DR   BioCyc; ECOL199310:C3709-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0009339; C:glycolate oxidase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:InterPro.
DR   GO; GO:0047809; F:D-2-hydroxy-acid dehydrogenase activity; IEA:RHEA.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0019154; F:glycolate dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
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; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR004490; GlcD.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   TIGRFAMs; TIGR00387; glcD; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; FAD; Flavoprotein; Membrane;
KW   Oxidoreductase.
FT   CHAIN           1..499
FT                   /note="Glycolate oxidase subunit GlcD"
FT                   /id="PRO_0000128182"
FT   DOMAIN          52..230
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
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