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Database: UniProt
Entry: A0A0M9YV31_9ACTN
LinkDB: A0A0M9YV31_9ACTN
Original site: A0A0M9YV31_9ACTN 
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}.
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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
//
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