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Database: UniProt
Entry: A9L091_SHEB9
LinkDB: A9L091_SHEB9
Original site: A9L091_SHEB9 
ID   A9L091_SHEB9            Unreviewed;       669 AA.
AC   A9L091;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE            EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN   OrderedLocusNames=Sbal195_0642 {ECO:0000313|EMBL:ABX47820.1};
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX47820.1, ECO:0000313|Proteomes:UP000000770};
RN   [1] {ECO:0000313|EMBL:ABX47820.1, ECO:0000313|Proteomes:UP000000770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195 {ECO:0000313|EMBL:ABX47820.1,
RC   ECO:0000313|Proteomes:UP000000770};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) 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   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004515}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004515}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004515}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000256|ARBA:ARBA00008040}.
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DR   EMBL; CP000891; ABX47820.1; -; Genomic_DNA.
DR   RefSeq; WP_006083149.1; NC_009997.1.
DR   AlphaFoldDB; A9L091; -.
DR   GeneID; 11770963; -.
DR   KEGG; sbn:Sbal195_0642; -.
DR   HOGENOM; CLU_014312_6_2_6; -.
DR   OMA; CHYFVDY; -.
DR   Proteomes; UP000000770; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR   NCBIfam; TIGR01812; sdhA_frdA_Gneg; 1.
DR   PANTHER; PTHR11632:SF71; FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT; 1.
DR   PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 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   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          7..411
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          469..598
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
FT   ACT_SITE        301
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ   SEQUENCE   669 AA;  73547 MW;  242CE03052CAEFE8 CRC64;
     MKIIYTDSLV IGAGLAGLRV AIATKERGLD TLVLSLIPAK RSHSAAAQGG MQASLGNTVK
     GMGDNEDIHF QDTVKGSDWG CDQDVARMFA HVAPKAIREL TNWGVPWSRI SAGPREVIMN
     AQRVTLNEAE EAHGLINARD FGGTKKWRTC YTADGTGHSL LYAVDNQAIS MGIPVHERIE
     ALSLIHDGKR CHGVIARCLV TGELRAYVAK STTIATGGYG KIYEISTNAT ICEGIGQALA
     LDTGVATLGN MEAVQFHPTA IVPAGILTTE GCRGDGGILR DKDGHRFMPD YEPEKKELAS
     RDVVSRRMTE HMRKGNGVES PYGPHLWLDI TQLGREHIET NLREVKEICD YFLGIDPCKD
     WIPVRPTQHY SMGGVRTNAT GESPQLKGLF SVGEAACWDM HGFNRLGGNS VAETVVGGMI
     IGKYVADFCE NNDLEIDTAL TQKFIDKLQQ EIDGLVEGNG TENPFQIKKE MQRIMMNYVG
     IFRNGPELDK AIKGLKDLLL RAKNLGLKCK KRHANPELVE ALRVTRMLKV ALTVACGAEA
     RTESRGAHSR EDYPQRNDKD WLNRTLATWP DAESLEPVLR YEALDVMKME LPPGYRGYGN
     DNTIAHPDTE KRVQEINQVL ARLGDDPDRN TLQRALMPYE LPSHLQAPNG RLSDTLAITP
     AQPVGNKPL
//
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