ID A0A0M9YV31_9ACTN Unreviewed; 653 AA.
AC A0A0M9YV31;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:KOU66957.1};
DE EC=1.3.5.1 {ECO:0000313|EMBL:KOU66957.1};
GN Name=sdhA {ECO:0000313|EMBL:KOU66957.1};
GN ORFNames=ADK55_04860 {ECO:0000313|EMBL:KOU66957.1};
OS Streptomyces sp. WM4235.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415551 {ECO:0000313|EMBL:KOU66957.1, ECO:0000313|Proteomes:UP000037699};
RN [1] {ECO:0000313|EMBL:KOU66957.1, ECO:0000313|Proteomes:UP000037699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM4235 {ECO:0000313|EMBL:KOU66957.1,
RC ECO:0000313|Proteomes:UP000037699};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOU66957.1}.
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; LGDE01000030; KOU66957.1; -; Genomic_DNA.
DR RefSeq; WP_053676202.1; NZ_LGDE01000030.1.
DR AlphaFoldDB; A0A0M9YV31; -.
DR PATRIC; fig|1415551.3.peg.1060; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000037699; Unassembled WGS sequence.
DR GO; GO:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
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; 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 PRINTS; PR00368; FADPNR.
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.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KOU66957.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037699}.
FT DOMAIN 48..453
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 518..652
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 342
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ SEQUENCE 653 AA; 72101 MW; 533C61F9B726A2B1 CRC64;
MSTPYADYAL GDPIADTKAP EGPIAERWDR RRFEAKLVNP ANRRKHTVIV VGTGLAGGAA
GATLAEQGYH VVQFCFSDSP RRAHSIAAQG GINAAKNYRN DGDSVHRLFY DTVKGGDFRA
RESNVHRLAQ ISVEIIDQCV AQGVPFAREY GGLLDTRSFG GVQVSRTFYA RGQTGQQLLL
GAYQALSRQI AAGNVEMHAR TEMLDLITID GVARGIVARD LVTGTIEAHY ADAVVLASGG
YGNVFYLSTN AMNSNATAVW RAHRRGAHFA NPCFTQIHPT CIPRTGDHQS KLTLMSESLR
NDGRIWVPKA EGDTRPAADI PEEERDYYLE RIYPSFGNLV PRDIASRAAK NVCDEGRGVG
PGGQGVYLDF ADAIRRMGKD KVAEKYGNLF DMYERITAEN PYEVPMRIYP AVHYTMGGLW
VDYDLQTTVP GLFAIGEANF SDHGANRLGA SALMQGLGDG YFVLPSTIND YLARRHAEGD
GDVLDDHHPE VAAVLRETRD CLAKLLAVDG DRTPDSFHRE IGELMWEYCG MARTEAGLRK
ALARIPEIRE EFWKRIKVPG SGAEFNQSLE KANRIVDYLE LAELMCLDAL HRAESCGGHF
REESQTPDGE AARRDEEFGY VAAWQYQGTG AAPVLHKEDL VFEYVHPTQR SYA
//