ID   GLCD_BACSU              Reviewed;         470 AA.
AC   P94535; Q795X0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 118.
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; Synonyms=ysfC; OrderedLocusNames=BSU28680;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Component of a complex that catalyzes the oxidation of
CC       glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)-
CC       lactate). Does not link directly to O(2), and 2,6-dichloroindophenol
CC       (DCIP) and phenazine methosulfate (PMS) can act as artificial electron
CC       acceptors in vitro, but the physiological molecule that functions as
CC       primary electron acceptor during glycolate oxidation is unknown.
CC       {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   -!- 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 several subunits
CC       including GlcD and GlcF. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P0AEP9}.
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000305}.
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; Z75208; CAA99599.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14828.1; -; Genomic_DNA.
DR   PIR; D69984; D69984.
DR   RefSeq; NP_390746.1; NC_000964.3.
DR   RefSeq; WP_004398865.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P94535; -.
DR   STRING; 224308.BSU28680; -.
DR   jPOST; P94535; -.
DR   PaxDb; P94535; -.
DR   PRIDE; P94535; -.
DR   EnsemblBacteria; CAB14828; CAB14828; BSU_28680.
DR   GeneID; 937770; -.
DR   KEGG; bsu:BSU28680; -.
DR   PATRIC; fig|224308.179.peg.3116; -.
DR   eggNOG; COG0277; Bacteria.
DR   InParanoid; P94535; -.
DR   OMA; CNDNMLA; -.
DR   PhylomeDB; P94535; -.
DR   BioCyc; BSUB:BSU28680-MON; -.
DR   Proteomes; UP000001570; 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; 3.30.465.10; -; 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; 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 membrane; FAD; Flavoprotein; Membrane; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..470
FT                   /note="Glycolate oxidase subunit GlcD"
FT                   /id="PRO_0000360827"
FT   DOMAIN          37..216
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   470 AA;  50936 MW;  3E315389A99A3D96 CRC64;
     MITKDVKEQL IQVSGPENFD DSNAGRLVYS YDATPQYQSM PDAVIAPRNT DEISRILTIC
     SEHRVPIVPR GSGTNLCGGT CPTEGGLVLL FKHMNQILEI DEENLTATVQ PGVITLDMIR
     AVESKGLFYP PDPSSMKIST IGGNINENSG GLRGLKYGVT RDYVIGLEVV LANGDIIRTG
     GKLAKDVAGY DLTRLFVGSE GTLGIVTEAI VKLVPKPETK KTLLALYENI DAAAQTVSDI
     IAAKIIPATL EFLDQPTLLV IEDYAKIGLP TSAKAVLLIE QDGPFETVER DMEKIEAICK
     KGDAVSVQTA QTEEEAFALT EARRSALSAL ARLKPTTILE DATVPRSEIA NMVKAINDIA
     AKYDISICTF GHAGDGNLHP TCTTDIRNKD EMERVEQAFA EIFEKAIELG GTITGEHGVG
     EMKAPYLEMK LKKEGIDAMK ALKAAFDPRN ILNPGKMFAK DARKRVVAER