ID J9DI39_9STAP Unreviewed; 587 AA.
AC J9DI39;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=SOJ_19950 {ECO:0000313|EMBL:EJX17706.1};
OS Staphylococcus sp. OJ82.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1202667 {ECO:0000313|EMBL:EJX17706.1, ECO:0000313|Proteomes:UP000006164};
RN [1] {ECO:0000313|EMBL:EJX17706.1, ECO:0000313|Proteomes:UP000006164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OJ82 {ECO:0000313|EMBL:EJX17706.1,
RC ECO:0000313|Proteomes:UP000006164};
RX PubMed=23105083; DOI=10.1128/JB.01653-12;
RA Sung J.S., Chun J., Choi S., Park W.;
RT "Genome Sequence of the Halotolerant Staphylococcus sp. Strain OJ82,
RT Isolated from Korean Traditional Salt-Fermented Seafood.";
RL J. Bacteriol. 194:6353-6354(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}.
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:EJX17706.1}.
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DR EMBL; ALPU01000010; EJX17706.1; -; Genomic_DNA.
DR RefSeq; WP_002507958.1; NZ_ALPU01000010.1.
DR AlphaFoldDB; J9DI39; -.
DR GeneID; 69846214; -.
DR PATRIC; fig|1202667.3.peg.1994; -.
DR Proteomes; UP000006164; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.820; -; 1.
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; 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 PIRSF; PIRSF000171; SDHA_APRA_LASPO; 2.
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 Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 6..392
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 452..579
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 587 AA; 65029 MW; 7994115EC0BBEE4F CRC64;
MAEKKVIVVG GGLAGLMSTI KAAEQGAHVD LFSLVPVKRS HSVCAQGGIN GAVNTKGEGD
SPAVHLDDTI YGGDFLANQP PVQAMTDAAP KIIHLLDRMG VMFNRTNEGL LDFRRFGGTM
HHRTAYAGAT TGQQLLYALD EQVRSFEVDG LVTKYEGWEF LGIVKDDDNM ARGIVAQNVT
TSGIESFGSD AVIMATGGPG IIFGKTTNSM INTGSAASIV YQQGAMYANG EFIQIHPTAI
PGDDKLRLMS ESARGEGGRI WTYKDGKPWY FLEEKYPDYG NLVPRDVATR EIFDVCVNQK
LGINGENMVY LDLSHKDPHE LDVKLGGIIE IYEKFTGDDP RKVPMKIFPA VHYSMGGLYV
DYDQMTNIKG LFAAGECDYS QHGGNRLGAN SLLSAIYGGT VAGPNAIEYI SNIETSYADL
DDSIFEKRVK EEQEKFDKLL NMQGSENAYK LHRELGEVMT ANVTVVRENK TLLETDKKIL
ELMERYNNID IEDTQTWSNQ AVFFTRQLWN MLVLARVITI GAYNRNESRG AHYKPEFPDR
NDEEWLKTTL ATYQGKTEAP KFTYEDVDIS LIPPRKRDYS TTSKGGK
//
