ID U5RP57_9CLOT Unreviewed; 468 AA.
AC U5RP57;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:AGY74352.1};
GN ORFNames=CAETHG_0117 {ECO:0000313|EMBL:AGY74352.1};
OS Clostridium autoethanogenum DSM 10061.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY74352.1, ECO:0000313|Proteomes:UP000017590};
RN [1] {ECO:0000313|EMBL:AGY74352.1, ECO:0000313|Proteomes:UP000017590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY74352.1};
RX PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT "Comparison of single-molecule sequencing and hybrid approaches for
RT finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT systems in industrial relevant Clostridia.";
RL Biotechnol. Biofuels 7:40-40(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP006763; AGY74352.1; -; Genomic_DNA.
DR RefSeq; WP_023161683.1; NZ_CP012395.1.
DR AlphaFoldDB; U5RP57; -.
DR KEGG; cah:CAETHG_0117; -.
DR PATRIC; fig|1341692.11.peg.114; -.
DR HOGENOM; CLU_017779_9_2_9; -.
DR Proteomes; UP000017590; Chromosome.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 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}.
FT DOMAIN 48..227
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 468 AA; 51191 MW; 6E94435DD5F59D56 CRC64;
MNTDLIKNSP EKVVESLRKV VGDDWVTNDL SQMQGYLYDE TETLLRPEAC KDCVVVKPAS
PEEISEVLKY ANKEVLPVIV RGGGTGVVAG AIPTQPSIIL SLERLNKVVE FDEKNLMITL
ESGATLSQLL EELNKNGKLF FPVHPGDEGA QVGGMVAANA GGTRAVKHGI MRNHVKALEV
VLATGEIITL GGKLLKNNMG YDLLQLMIGS EGTLGIITKV TLRLYARSKC NGTLLVSFNS
QREACDAVPE ILQEGITPLA IEYMDRVISE KAAEQLGTTW PAAKGSVDLM FILDECSEDD
LYSNSEKVVK ICEKHGSVDS IVAETEKDQS HLLQIRSNAY GPYKDNIADI MDVAVPPSSV
PDFFDDVKRL TKEYGNEIVS LGHIGDGNIH NFIMGDNGKL PTNYEQLKEE IYKTAIKYGG
TITAEHGTGK TRKKHMPLQF SQVEINIMEN IKRAFDPNSI LSPGNIVD
//
