ID   A4G1X5_HERAR            Unreviewed;       350 AA.
AC   A4G1X5;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Glycolate oxidase subunit GlcE {ECO:0000313|EMBL:CAL60512.1};
GN   Name=glcE {ECO:0000313|EMBL:CAL60512.1};
GN   OrderedLocusNames=HEAR0285 {ECO:0000313|EMBL:CAL60512.1};
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL60512.1, ECO:0000313|Proteomes:UP000006697};
RN   [1] {ECO:0000313|EMBL:CAL60512.1, ECO:0000313|Proteomes:UP000006697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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; CU207211; CAL60512.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4G1X5; -.
DR   STRING; 204773.HEAR0285; -.
DR   KEGG; har:HEAR0285; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_0_0_4; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000006697; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000006697}.
FT   DOMAIN          1..170
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   350 AA;  37450 MW;  B438EB492DDFE498 CRC64;
     MEEVVEQFKE TILAAGRQRQ ALCIRGGGTK DWYGQAPRGD ILDTRAYSGV VEYDPTELVI
     TVRAGTPLAE VEEVLAQQNQ ALAFDPPHFG PGATIGGMVA CGLSGPRRVA VGAARDFVLG
     AVLMDGKGEV LHFGGQVMKN VAGYDVSRLL TGSLGTLGLL LEVSLKVLPK PYAETSLRLE
     MPEEEAIRRL NEWGGQPLPI SASAWCDGAL VLRLSGAKAA ITAAQQTIGG EEIAGDDFWL
     ALREQSNEFF TQSNVLWRLS LPSVTPPLAL GEQLIEWGGA QRWLRSDADA ASIRAAAAQA
     GGHATLFRGG DKSVGVFQPL APAVARIHQN MKNAFDPEGI FNPGRMYPQY
//