ID A0A086YZZ0_9BIFI Unreviewed; 632 AA.
AC A0A086YZZ0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=BACT_0541 {ECO:0000313|EMBL:KFI39840.1};
OS Bifidobacterium actinocoloniiforme DSM 22766.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437605 {ECO:0000313|EMBL:KFI39840.1, ECO:0000313|Proteomes:UP000029015};
RN [1] {ECO:0000313|EMBL:KFI39840.1, ECO:0000313|Proteomes:UP000029015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22766 {ECO:0000313|EMBL:KFI39840.1,
RC ECO:0000313|Proteomes:UP000029015};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KFI39840.1}.
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DR EMBL; JGYK01000001; KFI39840.1; -; Genomic_DNA.
DR RefSeq; WP_033503271.1; NZ_JGYK01000001.1.
DR AlphaFoldDB; A0A086YZZ0; -.
DR STRING; 1437605.AB656_01305; -.
DR KEGG; bact:AB656_01305; -.
DR PATRIC; fig|1437605.7.peg.271; -.
DR eggNOG; COG1053; Bacteria.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000029015; Unassembled WGS sequence.
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; 4.10.80.40; succinate dehydrogenase protein 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: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:UP000029015};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 11..418
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 511..632
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 472..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 295
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 632 AA; 68271 MW; F115CA17BAAE52F9 CRC64;
MSPVNIEQEY DAVIVGAGAA GLSAALGLLE VADDNGEPLK LLVVSKLQPL RSHTGSAEGG
IAASLGNEEA DDWRWHYYDT VKGGDWLVDQ DAAKLLAQEA KATLIDLERA GVAFSRRADG
RISQRRFGGH TANYGGRPVK RAAYAADRIG HRILSSLWQQ CLKHGVAFAE EWYVCDLALS
DSGDEALGLV AWDERTGQVH AIRARKVILC TGGAGRLFHT SSNSYDLTGD GMSLALRAGL
QLEDMEFVQF HPTGLGHTGI LLSEASRAEG GVLRNAKGEA FMARYAPEHR DLAARDVVSR
AIVAETDQGR GVADPREPQG PKDCVWLDLR AIPAQDMRDK LPQVDETIRR YAGLDPTRDL
VPVKPTAHYM MGGLPIDLDG RIYRWNDGRR FPVAGLFAAG ECACVGVHGA NRLGGNSLLD
ACLFGRRAGR SAAQDILAER QSSSAAAPAQ QPDSVQSDRL DLLASQRRRE TAGLLDSATQ
TVDSAATPTT AGSANDGDAS TDSNPYQLIE SLGRLMDQAA AVRCDSDSLS SAQARLDGDL
SSQVENLSLH DPSPNFNQEL VAIFEVRNLT GLARAVLKSS LERQESRGSL SRLDFPRRDD
EHYLQHSLID ADGHISWQPV HIQDFPPGSR SY
//
