ID A0A0F2JDZ6_9FIRM Unreviewed; 574 AA.
AC A0A0F2JDZ6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=UF75_3018 {ECO:0000313|EMBL:KJR46613.1};
OS Desulfosporosinus sp. I2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1617025 {ECO:0000313|EMBL:KJR46613.1, ECO:0000313|Proteomes:UP000033442};
RN [1] {ECO:0000313|EMBL:KJR46613.1, ECO:0000313|Proteomes:UP000033442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I2 {ECO:0000313|EMBL:KJR46613.1,
RC ECO:0000313|Proteomes:UP000033442};
RA Mardanov A.V., Karnachuk O.V., Beletsky A.V., Kadnikov V.V., Ravin N.V.;
RL Submitted (FEB-2015) 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:KJR46613.1}.
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; JYNH01000058; KJR46613.1; -; Genomic_DNA.
DR RefSeq; WP_045575227.1; NZ_JYNH01000058.1.
DR AlphaFoldDB; A0A0F2JDZ6; -.
DR PATRIC; fig|1617025.3.peg.3156; -.
DR OrthoDB; 9806724at2; -.
DR Proteomes; UP000033442; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; IPR011280; Succ_DH/Fum_Rdt_flav_su.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR01811; sdhA_Bsu; 1.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF53; SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
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:UP000033442};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 4..389
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 449..574
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 282
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ SEQUENCE 574 AA; 63790 MW; 7A9148E6FA94A602 CRC64;
MSKVIVVGGG LAGLMATIKM AEAGTHVDLF SLVPVKRSHS VCAQGGINGA VNTKGEGDST
WLHFDDTVYG GDFLANQPPV KAMCDEAPGI IHLMDRMGVM FSRTPEGLLD FRRFGGTKFC
RTAFAGATTG QQLLYALDEQ VRRYEVEGMV QKYEQWELLS TVIEEGTCKG IVAQDLRSMG
IQSFAADAVI IATGGPGAVF GKSTNSTICT GSAVSALYQQ GVKYANGEFI QIHPTAIPGD
DKLRLMSESA RGEGGRIWTY KDGKPWYFLE EMFPDYGNLV PRDIATRAIY EVVFDQGLGL
NGENMVYLDL SHIDPEVLQR KLGGIIEIYE KFVGDDPKKV PMRIFPSVHY SMGGLWVDYD
QMTNIPGLFA AGECEYQYHG ANRLGANSLL SAIYGGMVAG PKVMEYIKKN KIQTPSGTEP
VFIKEKKLQD EQWAKILAMK GTENPYLLHK ELGDIMTLNV TVIRFNAKLE ETDVVLQKLM
KRWQNIGRSD NVEWGTQEGT FIRQLWNMLE LARVITLGAL RRNESRGGHY KPEYPERDDE
NFLKTTIASW TPSGPELSYE DVDVSLIPPR PRHY
//
