ID G0AUT2_9GAMM Unreviewed; 668 AA.
AC G0AUT2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN ORFNames=Sbal175_0471 {ECO:0000313|EMBL:AEG09766.1};
OS Shewanella baltica BA175.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=693974 {ECO:0000313|EMBL:AEG09766.1, ECO:0000313|Proteomes:UP000002249};
RN [1] {ECO:0000313|EMBL:AEG09766.1, ECO:0000313|Proteomes:UP000002249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA175 {ECO:0000313|EMBL:AEG09766.1,
RC ECO:0000313|Proteomes:UP000002249};
RX PubMed=22328742; DOI=10.1128/JB.06468-11;
RA Caro-Quintero A., Auchtung J., Deng J., Brettar I., Hofle M., Tiedje J.M.,
RA Konstantinidis K.T.;
RT "Genome sequencing of five Shewanella baltica strains recovered from the
RT oxic-anoxic interface of the Baltic Sea.";
RL J. Bacteriol. 194:1236-1236(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 -!- 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}.
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; CP002767; AEG09766.1; -; Genomic_DNA.
DR RefSeq; WP_006083366.1; NC_017571.1.
DR AlphaFoldDB; G0AUT2; -.
DR KEGG; sbb:Sbal175_0471; -.
DR HOGENOM; CLU_014312_6_2_6; -.
DR Proteomes; UP000002249; 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 REGION 638..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ SEQUENCE 668 AA; 73539 MW; 5E1950C0BAFB9409 CRC64;
MKLIYTDSLV VGAGLAGLRV AIASKERGLD TLVLSLIPAK RSHSAAAQGG MQASLGNAVK
GMGDDEDVHF QDTVKGSDWG CDQDVARMFA HCAPKAVREL ATWGVPWSRV SAGPRDVIVN
AQKVTLHEAQ EAHGLINARD FGGTKKWRTC YTADGTGHSL LYAMDNKAIS MDIPVHERIE
ALALIHDGKR CHGVIARCLI TGELRAYVAK STTIATGGYG RIYEVSTNAI ICEGIGQALA
LETGVARLGN MEAVQFHPTA IVPVGILTTE GCRGDGGLLR DKDGYRFMPD YEPDKKELAS
RDVVSRRMTE HIRKGKGVDS PYGPHLWLDI TLLGRKHIET NLREVQEICE NFLGIDPAKD
WIPVRPTQHY SMGGIRTNAT GESPQLKGLF SVGEAACWDM HGFNRLGGNS LAETVVGGMI
IGKYVADFCE NNSLEIDTQL AERFMQQVQS EIDLLIEGDG HESAFALKRE MQRIMMDYVG
IFRNGPELDK AVAELKVLLE RSRKLGLKCK KRHANPELVE ALRVKRMLKV ALTVACGAAA
RTESRGAHAR EDYPQRNDRD WLNRTLASWP DPDALEPVLN YEALDVMKME LPPGYRGYGI
NNAIVHPNTE KREQEIANIL AELGDDADRY QRQRALMPFE LPESLQPNNE RLSDTLKSPS
ANALGEKS
//
