SDHA_PARDE
ID SDHA_PARDE Reviewed; 600 AA.
AC Q59661;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Succinate dehydrogenase flavoprotein subunit;
DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P0AC41};
GN Name=sdhA;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RA Dickins M.A., Dhawan T., Gunsalus R.P., Schroeder I., Cecchini G.;
RT "Cloning, sequencing, and expression of the succinate-ubiquinone
RT oxidoreductase (SdhCDAB) operon from Paracoccus denitrificans.";
RL Submitted (SEP-1995) 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:0000250|UniProtKB:P0AC41};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P0AC41};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC from succinate (bacterial route): step 1/1.
CC {ECO:0000250|UniProtKB:P0AC41}.
CC -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC flavoprotein, an iron-sulfur, cytochrome b-556, and a hydrophobic
CC anchor protein. {ECO:0000250|UniProtKB:P0AC41}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AC41}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P0AC41}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P0AC41}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000305}.
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DR EMBL; U31902; AAA75177.1; -; Genomic_DNA.
DR PIR; T46880; T46880.
DR RefSeq; WP_011746914.1; NZ_PPGA01000002.1.
DR AlphaFoldDB; Q59661; -.
DR SMR; Q59661; -.
DR OMA; DPIPIQP; -.
DR UniPathway; UPA00223; UER01005.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 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; IPR011281; Succ_DH_flav_su_fwd.
DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR PANTHER; PTHR11632; PTHR11632; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR01816; sdhA_forward; 1.
DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; FAD; Flavoprotein;
KW Membrane; Oxidoreductase; Transport; Tricarboxylic acid cycle.
FT CHAIN 1..600
FT /note="Succinate dehydrogenase flavoprotein subunit"
FT /id="PRO_0000158655"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AC41"
FT BINDING 17..22
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0AC41"
FT BINDING 40..55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0AC41"
FT BINDING 224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0AC41"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC41"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC41"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC41"
FT BINDING 390
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0AC41"
FT BINDING 401
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AC41"
FT BINDING 406..407
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0AC41"
FT MOD_RES 48
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:P0AC41"
SQ SEQUENCE 600 AA; 65616 MW; E8446E4FB6D8F829 CRC64;
MAAYKYETHE YDVVVVGAGG AGLRATLGMA EQGLRTACVT KVFPTRSHTV AAQGGIAASL
SNMGPDNWQW HMYDTVKGSD WLGDTDAMEY LAREAPKAVY ELEHYGVPFS RTEEGKIYQR
PFGGHTTEFG EGPPVQRTCA AADRTGHAIL HTLYGQSLKE KAEFFIEYFA LDLIITDGAC
TGVVCWKLDD GTIHVFNAKM VVLATGGYGR AYFSATSAHT CTGDGGGMVA RAGLPLQDME
FVQFHPTGIY GSGCLITEGA RGEGGYLTNS EGERFMERYA PTYKDLASRD VVSRCITIEI
REGRGVGPHK DHMHLNLMHL PPESLAERLP GISESAKIFA GVDVTREPIP ILPTVHYNMG
GIPTNYWGEV LNPTQDNPDQ VFPGLMAVGE AGCASVHGAN RLGSNSLIDL VVFGRAAAIR
AGQVIDREAQ IPTTNKEQVD KALDRFDRIR NADGSVSTAD LRLEMQRTMQ ADAAVFRTDK
TLAEGVDKMR VIAGKLSDLK VTDRSLIWNS DLMETLELTN LMPNALATIV AAEARKESRG
AHAHEDYPER DDANWRKHSL AWIEGNDVKL AYRPVHLEPL TRQDEGGIDL KKIAPKARVY
