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Database: UniProt
Entry: G4Q3V7_ACIIR
LinkDB: G4Q3V7_ACIIR
Original site: G4Q3V7_ACIIR 
ID   G4Q3V7_ACIIR            Unreviewed;       466 AA.
AC   G4Q3V7;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=FAD-linked oxidase {ECO:0000313|EMBL:AEQ23023.1};
GN   Name=glcD {ECO:0000313|EMBL:AEQ23023.1};
GN   OrderedLocusNames=Acin_1812 {ECO:0000313|EMBL:AEQ23023.1};
OS   Acidaminococcus intestini (strain RyC-MR95).
OC   Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC   Acidaminococcus.
OX   NCBI_TaxID=568816 {ECO:0000313|EMBL:AEQ23023.1, ECO:0000313|Proteomes:UP000007093};
RN   [1] {ECO:0000313|EMBL:AEQ23023.1, ECO:0000313|Proteomes:UP000007093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RyC-MR95 {ECO:0000313|EMBL:AEQ23023.1,
RC   ECO:0000313|Proteomes:UP000007093};
RX   PubMed=22123762; DOI=10.1128/JB.06301-11;
RA   D'Auria G., Galan J.C., Rodriguez-Alcayna M., Moya A., Baquero F.,
RA   Latorre A.;
RT   "Complete genome sequence of Acidaminococcus intestini RYC-MR95, a Gram-
RT   negative bacterium from the phylum Firmicutes.";
RL   J. Bacteriol. 193:7008-7009(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP003058; AEQ23023.1; -; Genomic_DNA.
DR   RefSeq; WP_009015858.1; NC_016077.1.
DR   AlphaFoldDB; G4Q3V7; -.
DR   STRING; 568816.Acin_1812; -.
DR   GeneID; 72309680; -.
DR   KEGG; ain:Acin_1812; -.
DR   PATRIC; fig|568816.4.peg.1760; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_9_2_9; -.
DR   InParanoid; G4Q3V7; -.
DR   Proteomes; UP000007093; 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   Gene3D; 3.30.70.2740; -; 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; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR   PANTHER; PTHR42934:SF2; 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:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007093}.
FT   DOMAIN          44..223
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   466 AA;  50865 MW;  E939E529B5162776 CRC64;
     MEHYEKLTES TIEELKAIVG EKYVLTTPET LETYQTDQET DSRFFHVPEA VAAPGSTEEV
     AAIMKLANKR HFSVTPRSGG TSVSDGAIAV CGGIVMLMER MNRILEVNPD GMYMVVEAGA
     RTLDVQEAAK KEGLFYAGDP CSADSCLIGG NLATNAGGDK AVRYGTTRSQ VHAIEVVLPT
     GEIAHLGART KKNTTGFCLD QLVLGSEGTL GVITKATLKL LPIAPYRSDV LLVFTDPRKA
     TSLVPILLKA GLDPTSVEFM DHGFVQASSD YSKIRLSHYD DGCYVILTLE TFDEDEMDKK
     LIKVDELAQA HGAVEVSLAD DRVWTIRKNC LEATRILSRV STSDDFVFPL DKISDAIMDL
     SELAATYPFR VFTLAHAGDG NLHFNILKGE LSDEAWEETL SSFHEKAYAY VYAHDGLLSG
     EHGIGAKKVG QLERLTDPGQ MFMMTAIKKA LDPLDVLNPG KVIARY
//
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