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Database: UniProt
Entry: A0A3B0C3E6_9BACL
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Original site: A0A3B0C3E6_9BACL 
ID   A0A3B0C3E6_9BACL        Unreviewed;       572 AA.
AC   A0A3B0C3E6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=FAD-binding protein {ECO:0000313|EMBL:RKN78277.1};
GN   ORFNames=D7M11_23510 {ECO:0000313|EMBL:RKN78277.1};
OS   Paenibacillus ginsengarvi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=400777 {ECO:0000313|EMBL:RKN78277.1, ECO:0000313|Proteomes:UP000282311};
RN   [1] {ECO:0000313|EMBL:RKN78277.1, ECO:0000313|Proteomes:UP000282311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 13059 {ECO:0000313|EMBL:RKN78277.1,
RC   ECO:0000313|Proteomes:UP000282311};
RX   PubMed=17684262; DOI=10.1099/ijs.0.64906-0;
RA   Yoon M.H., Ten L.N., Im W.T.;
RT   "Paenibacillus ginsengarvi sp. nov., isolated from soil from ginseng
RT   cultivation.";
RL   Int. J. Syst. Evol. Microbiol. 57:1810-1814(2007).
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:RKN78277.1}.
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DR   EMBL; RBAH01000019; RKN78277.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0C3E6; -.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000282311; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal 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; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR030664; SdhA/FrdA/AprA.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR11632:SF82; FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282311}.
FT   DOMAIN          9..393
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          457..554
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        290
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ   SEQUENCE   572 AA;  62619 MW;  5A90E9196AF47CAD CRC64;
     MEPLQLQADV LIVGSGAAGM MAARAAADEG ARVLLIDKSL IGRGGATILA QMTVAVALGE
     ADDDNTEIHF EDTMKGSRGL ADPAIVRAIV ERGPEVILEA ETYGVNWART AEGKRSQAFA
     PGHSKSRCVY VDILNTGGAT AAGLKKAIWK EEKIRRYKNV MVTNIVVDEQ GRAVGAVGFD
     IEQYRPVSVE ASSVILATGG LTEVYERNSA SANMTGDGYM LAAEAGAELR DMEMVQFFPI
     AHLFPPLVGI DPIMWDPFRY KLGGRLLNGN GEEFMDRYNG EVSGQYTATR DQTTLAIFRE
     VEEGRGTQHG GAYLDFRMVP EQKLKEAFGP VIDILRSQNV DLTQDMVEVA PMAHFMLGGV
     RVDEQMRTRV PGLLAAGELI YGMHGANRLS GNAITEALVT GRIAGETAAR EAAAHSGEPS
     KRAVIDEALA KEMNRLEQFW HPQPAGRDQS SLQAFKRKFQ HVMWKGAGPL RTEAGLLQAL
     DEVRALGEEL EQIALARQST YVLPLVEKVE AARMLQTGEA IILGALERKE SRGAHVRLDY
     EETNEQPVSY TFRWNDRRQW EIQPNVLQGT NP
//
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