ID I3WIN2_BIFBI Unreviewed; 671 AA.
AC I3WIN2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN Name=sdhA {ECO:0000313|EMBL:AFL04745.1};
GN ORFNames=BBB_1153 {ECO:0000313|EMBL:AFL04745.1};
OS Bifidobacterium bifidum BGN4.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=484020 {ECO:0000313|EMBL:AFL04745.1, ECO:0000313|Proteomes:UP000006173};
RN [1] {ECO:0000313|EMBL:AFL04745.1, ECO:0000313|Proteomes:UP000006173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGN4 {ECO:0000313|EMBL:AFL04745.1,
RC ECO:0000313|Proteomes:UP000006173};
RX PubMed=22887663; DOI=10.1128/JB.00988-12;
RA Yu D.S., Jeong H., Lee D.H., Kwon S.K., Song J.Y., Kim B.K., Park M.S.,
RA Ji G.E., Oh T.K., Kim J.F.;
RT "Complete Genome Sequence of the Probiotic Bacterium Bifidobacterium
RT bifidum Strain BGN4.";
RL J. Bacteriol. 194:4757-4758(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + succinate = a quinol + fumarate;
CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000030};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040}.
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DR EMBL; CP001361; AFL04745.1; -; Genomic_DNA.
DR RefSeq; WP_014760384.1; NC_017999.1.
DR AlphaFoldDB; I3WIN2; -.
DR KEGG; bbf:BBB_1153; -.
DR PATRIC; fig|484020.3.peg.1135; -.
DR HOGENOM; CLU_014312_6_2_11; -.
DR Proteomes; UP000006173; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
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; IPR003952; FRD_SDH_FAD_BS.
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; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF89; SUCCINATE DEHYDROGENASE [IRON-SULFUR SUBUNIT] (SUCCINIC DEHYDROGENASE)-RELATED; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1.
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.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AFL04745.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006173};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 11..433
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 538..671
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 489..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 300
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 671 AA; 71753 MW; E0760813FEE1AD9A CRC64;
MSPKHVEEMY DAVIVGAGAA GLSAALGLMH SPDIEQLKES GIEPKVLVIS KLQPLRSHTG
SAEGGIAASL GNVEQDDWHW HYYDTVKGGD WLVDQDAAKL LAEYAPQTVI NLERMGVAFS
RTDDGHIAQR RFGGHTADFG KMPVRRAAYA ADRIGHQILH SLWQQCVAAG IEFAEEWYVT
DVVLDKSGSA VAGVVAYDTH AGVTHAIHAH NVMFATGGAG RLFHTTSNSW DLTGDGMALA
LSAGLQLEDI EFVQFHPTGL AHTGILLSEA ARAEGGVLRN ADGEAFMERY APEHRDLAAR
DVVSRSIMAE IDGGRGVADP KDPDGPKDCV WLDMTGIDPD HMNAVLPQVV ETIKAYANLD
PAKDMVPVKP TAHYTMGGIP ITTDGEVYRW AESGSQNVDA VSGTRTVVEG LFAAGECSCV
SVHGANRLGG NSLLDACLFG TRAGESLAAR IAQSPVDDPM RDADADDGPA EAAAALVDDV
ARSRKQDVAT MLAGRPDVDD DAADDTSDGM PQTAELGGSD ASAQPGSKED NPYRLAADLG
TLMEHALAVR CDARSISEAL NLLDTVIRPR ASRLTAHSET PAFNQEITAI WEVRHLTLLA
EAMLRASEAR HESRGSLQRL DYPARDDERF LAHSMIGMAD AADAEASSAP HASILWQSVH
IDDFPPKTRE Y
//
