ID D7GNZ6_9FIRM Unreviewed; 478 AA.
AC D7GNZ6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=FAD/FMN-containing dehydrogenases {ECO:0000313|EMBL:CBL42531.1};
DE EC=1.1.3.15 {ECO:0000313|EMBL:CBL42531.1};
GN ORFNames=CK3_30750 {ECO:0000313|EMBL:CBL42531.1};
OS butyrate-producing bacterium SS3/4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL42531.1, ECO:0000313|Proteomes:UP000008961};
RN [1] {ECO:0000313|EMBL:CBL42531.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL42531.1,
RC ECO:0000313|Proteomes:UP000008961};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SS3/4.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL42531.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL42531.1,
RC ECO:0000313|Proteomes:UP000008961};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FP929062; CBL42531.1; -; Genomic_DNA.
DR AlphaFoldDB; D7GNZ6; -.
DR KEGG; bprs:CK3_30750; -.
DR PATRIC; fig|245014.3.peg.1633; -.
DR HOGENOM; CLU_017779_9_2_9; -.
DR BioCyc; BBAC245014:G1314-2653-MONOMER; -.
DR Proteomes; UP000008961; Chromosome.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
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; 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 Oxidoreductase {ECO:0000313|EMBL:CBL42531.1}.
FT DOMAIN 42..221
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 478 AA; 52088 MW; 0B00E243CA5B0427 CRC64;
MAKKYNEVTP EILEQFKAIV PGKVYAGEEI NSDYFHDEMP IYGKGAPEVV IEATTTEDIA
AIVKVCYENS IPVIPRGAGT GLTGAAVAVD GGVMIDMSKM NKILDYDLEN FVVRLEPGVL
LNDLAEDAQK QGLLYPPDPG EKFATLGGNV STNAGGMRAV KYGCTRDYVR AMTVVLPTGE
IVKLGATVSK TSTGYSLLNL MIGSEGTLGI ITELTLKLIP APKETISLII PYENLEDCIA
TVPKFFMNHF QPQALEFMEK EIVLASERYL GKSVFPKQVE GVDIGAYLLV TFDGDNMEQL
EELTEQAAEV VLDAGAVDVL VADTPAKKKD AWAARSSFLE AIEAETKLLD ECDVVVPVNQ
IAKYLTYVKG ASEKYDFEVK SFGHAGDGNL HIYTCANDMD EETFKKQVSE FMADIYRKAA
ELGGLISGEH GIGFGKKGYL AEFAGPVNMR LMRGIKETFD PKMILNPGKI CYDPKEEA
//
