ID A0A0M2U0Z8_9FIRM Unreviewed; 458 AA.
AC A0A0M2U0Z8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=FAD-binding protein {ECO:0000313|EMBL:KKM09805.1};
GN ORFNames=SY88_16540 {ECO:0000313|EMBL:KKM09805.1};
OS Clostridiales bacterium PH28_bin88.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1605376 {ECO:0000313|EMBL:KKM09805.1, ECO:0000313|Proteomes:UP000034222};
RN [1] {ECO:0000313|EMBL:KKM09805.1, ECO:0000313|Proteomes:UP000034222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Robbins S., Tyson G.;
RT "High quality genome sequence of Candidatus Suratobacter aromatica.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKM09805.1}.
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DR EMBL; LAKY01000058; KKM09805.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2U0Z8; -.
DR STRING; 1605376.SY88_16540; -.
DR PATRIC; fig|1605376.3.peg.4415; -.
DR Proteomes; UP000034222; Unassembled WGS sequence.
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; 3.30.70.2190; -; 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 Reference proteome {ECO:0000313|Proteomes:UP000034222}.
FT DOMAIN 35..214
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 458 AA; 49406 MW; 709791A2EE9373A8 CRC64;
MKQEVISRMH QIMNKEQILT NLEDRMTYAY DGTMQTGVPG VVVFPRTTRQ VAEALRLANR
EKIPVYPRGA GTGLSGGSVP EQGGIALVLT DMNRILEVDT GNLLAVVEPG VVTEALQQEV
ERVGLFYPPD PGSLKSCTIG GNIAENAGGP RALKYGVTRD YVLGLEVVTP TGEILRTGGK
TVKNVTGYDL TRLMTGSEGT LGVVTRAVLR LIPRPQDVRT AMAVFATVDG AAEAVAEVSR
RGILPTTLEL MDDVTIRCVE NYLHMGLPVD AGAILLIEVD GFRPAVDEAI ITVEKVCREL
GATGVEVAAG PAEREELWRA RRAVSAAIVQ LKPTKISEDA TVPRSRVPEM VRRLKAIAQK
YDLTMAIFGH AGDGNLHPNI LADRRDPEEM ARVELAVEEL FRAAMELEGT LSGEHGIGSM
KAPYLPLEVG ETGMRVMRGI KAALDPNNIL SPGKMLWG
//