ID A6NP91_9FIRM Unreviewed; 606 AA.
AC A6NP91;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:EDN01996.1};
GN ORFNames=BACCAP_00029 {ECO:0000313|EMBL:EDN01996.1};
OS Pseudoflavonifractor capillosus ATCC 29799.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudoflavonifractor.
OX NCBI_TaxID=411467 {ECO:0000313|EMBL:EDN01996.1, ECO:0000313|Proteomes:UP000003639};
RN [1] {ECO:0000313|EMBL:EDN01996.1, ECO:0000313|Proteomes:UP000003639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDN01996.1,
RC ECO:0000313|Proteomes:UP000003639};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDN01996.1, ECO:0000313|Proteomes:UP000003639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDN01996.1,
RC ECO:0000313|Proteomes:UP000003639};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Pseudoflavonifractor capillosus ATCC 29799.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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:EDN01996.1}.
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DR EMBL; AAXG02000001; EDN01996.1; -; Genomic_DNA.
DR AlphaFoldDB; A6NP91; -.
DR STRING; 411467.BACCAP_00029; -.
DR eggNOG; COG1053; Bacteria.
DR Proteomes; UP000003639; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1010.20; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR007329; FMN-bd.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF04205; FMN_bind; 1.
DR SMART; SM00900; FMN_bind; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003639}.
FT DOMAIN 43..117
FT /note="FMN-binding"
FT /evidence="ECO:0000259|SMART:SM00900"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 63012 MW; 4CC710750C350E96 CRC64;
MLSLAACGAP AGEGTPSPSI TPSASAPAQG AFTDGTYTGS ANGNNGPIEV SVTVENGNIT
DVTIVSHEET AGISDPALED IPKAIVEQQS TQVDAVAGAT MTSNGIMAAV ENALNGGGEE
ETTAEITIDP DVIVVGAGLA GMVASVRAAE VGAKVLVLEQ NFRIGGSANT AGGSISGAGF
EAQKAAGIED SPEKFYDDFI TMGGGEQNLN PAIAKVHAER SGAAIDWLKN DIGVEFSDQV
DSGGYLTMNT DRVTYTAGGA SSGGATYFLK ALSAKLDEYI AAGQAQLMLD TMVTDVVLDA
DKNIIGVKIG DQEVLAPSTI IATGGYGYSE EWLKEFNFTN ITSNDPNTAI GSGYDFARTA
GAAFDNMDYC SCYGGSVPVS GFQASLRCNI NYNGAVWINT AGERVFNEPA ATSMDKRTVW
RTTDQNIIYV VFTEQMLQEA EAQEQALFTG MMSNSAAFTT QEKIDELLEQ GYMFKADTLE
DLAAQIGADK LPETIAKYNE DVAAGADSVF GRTDNLVAFE EGPYYAVYTV PYLMMTAGGP
RINENAQMVR EDGSVVGGAY LAGEIIGSAN IAGHNTIGGI GHGMCATWGK YSAELAAANA
GIEVKE
//