ID A0A089L5K1_9BACL Unreviewed; 654 AA.
AC A0A089L5K1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=FAD-binding protein {ECO:0000313|EMBL:AIQ55375.1};
GN ORFNames=R70331_30465 {ECO:0000313|EMBL:AIQ55375.1};
OS Paenibacillus sp. FSL R7-0331.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ55375.1, ECO:0000313|Proteomes:UP000029487};
RN [1] {ECO:0000313|EMBL:AIQ55375.1, ECO:0000313|Proteomes:UP000029487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ55375.1,
RC ECO:0000313|Proteomes:UP000029487};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009284; AIQ55375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A089L5K1; -.
DR STRING; 1536773.R70331_30465; -.
DR KEGG; paee:R70331_30465; -.
DR eggNOG; COG1053; Bacteria.
DR eggNOG; COG3976; Bacteria.
DR HOGENOM; CLU_011398_4_0_9; -.
DR Proteomes; UP000029487; Chromosome.
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; 2.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000029487};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..654
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001846145"
FT DOMAIN 62..137
FT /note="FMN-binding"
FT /evidence="ECO:0000259|SMART:SM00900"
FT REGION 21..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 67843 MW; D894EE854AF52363 CRC64;
MFRVSISLIM LLAVIGGCSS NSADPEATEQ PAASPEATQQ AADDSGVPAS FKAGTYKAEA
DGKDGTIQVE VTLDDKQTIT DIKVLSQTET AGIGVEAIDK IREQIITGQT LKVDAVSGAS
ESSNAILAAV ENALNQAGGD VAAFKSREVA KAGAGKTEQL SADVVVVGAG ASGVSAAVSA
ADTGAKVILI EKTATIGGAS NLSWAGKFYN SSAAVSSGLK VNVEKEISDW IVNNHWRVDA
AAIRQYVTKS GETYDWLTGK GYSTTFINFG GEQLHMLPAY ETRQELLRAM LAESVEKGGG
QILTETTAKK LITGAGGEVT GVIAEKADGT TLEITGKSIV MATGGYAANA EMVKEAFGFE
GVNGGLGQNI GEGLKMAWEA GAKVPDNFGG QMLHQTLARA TEKLKAEYEP FQASYPLMTT
YLPTFMNVGP SGARFRDEAA TLTAVAAANT SAFNGAYHLV IVSKSQLDAL AAKGMNGVKA
PGLPGMPPEF YAAFADKFTL ENPWQNAEKV FDSMAANGDG YKGSTIEELA ANAGMDAAVF
KDAFTKYEAA AKSGVDSEFG KAKEYLLPMG ESGPYYAVIA EINNLGSVGG LIVNTKFQVL
NDKRVPVKGL YAVGLESEGV MYNDTYVGNG VGLGYSFTSG RLGGEDAAAA ALGQ
//
