ID F7V7C7_CLOSS Unreviewed; 472 AA.
AC F7V7C7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN OrderedLocusNames=CXIVA_25860 {ECO:0000313|EMBL:BAK48555.1};
OS Clostridium sp. (strain SY8519).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK48555.1, ECO:0000313|Proteomes:UP000008937};
RN [1] {ECO:0000313|Proteomes:UP000008937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937};
RX PubMed=21914882; DOI=10.1128/JB.05637-11;
RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT "Complete genomic sequence of the O-desmethylangolensin-producing bacterium
RT Clostridium rRNA cluster XIVa strain SY8519, isolated from adult human
RT intestine.";
RL J. Bacteriol. 193:5568-5569(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AP012212; BAK48555.1; -; Genomic_DNA.
DR RefSeq; WP_013978508.1; NC_015737.1.
DR AlphaFoldDB; F7V7C7; -.
DR STRING; 1042156.CXIVA_25860; -.
DR KEGG; cls:CXIVA_25860; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_9; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000008937; 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; 3.30.70.2190; -; 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:UP000008937}.
FT DOMAIN 41..219
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 472 AA; 51058 MW; 55D9E3CF6020B556 CRC64;
MEYNQVTEEM TAKLRASVTG TVYTGAEISE DYSHDEYEVH GHCMPEAVVV VKSTEDVSAV
CRICYEYEVP FLVRGAGTGL AGGCVPIAGG VVIDMQKMNQ ILGIHKEDQV IRVQAGALIQ
DLQAACLAED MIYPPDPGEK LATVGGNVAT NAGGMRACKY GSTRDWVLAM TVVMPRGDIM
EFGAEVSKSA SGYSLMNLIS GSEGTLGIIT ELSMKIAPRP AGTISLLAPF ADVETCISCV
ASVKNANLDP QCLEFMDRSN VDAVHHYLKR TVFPTEMEGT QAGAYLLVNF EIFSDEEAEG
IMERAAEVFL ENGALDVVVY DTPAALHAAW EVRGSVLEAI LEDFDLTDEV DIVVPVSKLA
EYIIYCQNLE VPEGMEIRLA GHAGNGNLHV SVCAKDMEQG EFEEKIRGIF DLLYQKGIEL
KGCVSGEHGI GSANIDRLEQ FLGKPQMELM TAIKQACDPK MLLNPGKVCF SL
//
