ID A0A0A7I8A1_9BIFI Unreviewed; 619 AA.
AC A0A0A7I8A1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=AH67_05830 {ECO:0000313|EMBL:AIZ16482.1};
OS Bifidobacterium pseudolongum PV8-2.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1447715 {ECO:0000313|EMBL:AIZ16482.1, ECO:0000313|Proteomes:UP000030636};
RN [1] {ECO:0000313|EMBL:AIZ16482.1, ECO:0000313|Proteomes:UP000030636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV8-2 {ECO:0000313|EMBL:AIZ16482.1,
RC ECO:0000313|Proteomes:UP000030636};
RX PubMed=25614573;
RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Stevens M.J.,
RA Jans C.;
RT "Bifidobacterium pseudolongum Strain PV8-2, Isolated from a Stool Sample of
RT an Anemic Kenyan Infant.";
RL Genome Announc. 3:0-0(2015).
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; CP007457; AIZ16482.1; -; Genomic_DNA.
DR RefSeq; WP_022858653.1; NZ_CP007457.1.
DR AlphaFoldDB; A0A0A7I8A1; -.
DR STRING; 1447715.AH67_05830; -.
DR KEGG; bpsp:AH67_05830; -.
DR HOGENOM; CLU_014312_6_2_11; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000030636; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
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 InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF51; SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL; 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 Reference proteome {ECO:0000313|Proteomes:UP000030636};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 11..423
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 498..619
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 300
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 619 AA; 66723 MW; D70386AFB1955F6E CRC64;
MSPKHIEELY DAVIVGAGAA GLSAALGLYR SDAMQALRAQ GSEPKILVVS KLQPLRSHTG
SAEGGIAASL GNVEPDNWHW HYFDTVKGGD WLVDQDAARV LAQEAPQTVI NLERSGVAFS
RTKDGLIAQR RFGGHTREFG QEPVKRAAYS ADRIGHQILH TLWQQCAAYG VQFAEEWYVS
DLVLDETCSR VAGIVAYDTH AGTTHAIAAT HVIMATGGAG RLFHTTSNSY DLTGDGMALA
LQAGLQLEDI EFMQFHPTGL AHTGILLSEA SRAEGGVLRN ADGEAFMARY APEHKDLAAR
DVVSRAMRAE IEAGRGVADP KDPLGPQDCL WLDLTELDAQ HMRAVLPQVV QTVEDYAGLD
PSRDYIPVKP TAHYTMGGIP TTLNGQVYTW SDGERHIVDG LYAAGECACV SVHGANRLGG
NSLLDACLFG TRAGAMVALR LLDRPAAASG VDPALTEALD AAQARRDAQI TDMLATTPPD
DVETSEQPTD NAYQLMADLG SVMESGVAVT CDNASITQAL HRLEADLEPR AHALRTHSDA
RTFNQEITAI WEARHLVELA RTMLAATSAR HESRGSLYRT DFPQRDDTGF LAHSMTAAGQ
TPLWQPVHIV NIEPGTRAY
//
