ID G2DG32_9GAMM Unreviewed; 628 AA.
AC G2DG32;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=succinate dehydrogenase {ECO:0000256|ARBA:ARBA00012792};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN Name=sdhA3 {ECO:0000313|EMBL:EGV50433.1};
GN ORFNames=Rifp1Sym_dd00140 {ECO:0000313|EMBL:EGV50433.1};
OS endosymbiont of Riftia pachyptila (vent Ph05).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1048808 {ECO:0000313|EMBL:EGV50433.1, ECO:0000313|Proteomes:UP000004491};
RN [1] {ECO:0000313|EMBL:EGV50433.1, ECO:0000313|Proteomes:UP000004491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(2011).
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 -!- 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:EGV50433.1}.
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DR EMBL; AFOC01000083; EGV50433.1; -; Genomic_DNA.
DR RefSeq; WP_005965239.1; NZ_AFOC01000083.1.
DR AlphaFoldDB; G2DG32; -.
DR PATRIC; fig|1048808.3.peg.2606; -.
DR Proteomes; UP000004491; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
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 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 ECO:0000313|EMBL:EGV50433.1}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 7..420
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 480..625
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ SEQUENCE 628 AA; 69591 MW; BC981907CD4BE4B4 CRC64;
MRAQRRVIVV GGGLGGLWAA LTLAEHGVQV DLFSLFEVKR SHSACAQGGI NAVLDSKGEH
DSIEQHILDT IKGGAYLANQ PPIKSLCEAA PGLIRTFERM GVTFSRTPEG LMDLRLFGGV
KKRRTCFAGA STGQQLLYGV DEQVRAQEVA GRIRKHEWWE FLSLVKDPDD NCRGIVAMDL
RSLDVVSFRA DAVILATGGL GLIYGRSTNS TNSTGAAASR VYQQGAHFAN GEFIQFHPTT
MLGEDKTRLM SEAARGEGGR IWVPKDLHDK RMPNDIPESA RWYFLEEWYP SYGNTVPRDV
ASRAIWKLVR ELGYGIGGED AVYLDLTHLD PDFIETRLGA ILDIYRKFQG VDPVKEPMKI
FPGIHYSMGG LWIDFETDAT SGGIRWDSPR NHATNIPGLY ACGECDYGYH GANRLGANSL
LSASYSGQVA GEAVASYLQG IESGCDTVDE AHYSAEQQRQ TEINQRLMRA NGPENPYALH
RELGMIMATH VNVVRDNPGL DQAAEALQKL EARFWKLCLG ERSGWANQSL VYARQVHDMI
VLGRVITAGA RARDESRGSH YKPAFNLEIP QGKFPGDPEF EAYRKAWKEN NDNWLKTTIA
EHNSAGPRIS YEAVDLSIIA PEEPRDYR
//
