ID A0A1Q5N793_9ACTN Unreviewed; 665 AA.
AC A0A1Q5N793;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:OKK22314.1};
DE EC=1.3.5.1 {ECO:0000313|EMBL:OKK22314.1};
GN Name=sdhA {ECO:0000313|EMBL:OKK22314.1};
GN ORFNames=AMK16_03930 {ECO:0000313|EMBL:OKK22314.1};
OS Streptomyces sp. CB00455.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703927 {ECO:0000313|EMBL:OKK22314.1, ECO:0000313|Proteomes:UP000185643};
RN [1] {ECO:0000313|EMBL:OKK22314.1, ECO:0000313|Proteomes:UP000185643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB00455 {ECO:0000313|EMBL:OKK22314.1,
RC ECO:0000313|Proteomes:UP000185643};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKK22314.1}.
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DR EMBL; LIVQ01000001; OKK22314.1; -; Genomic_DNA.
DR RefSeq; WP_073908569.1; NZ_LIVQ01000001.1.
DR AlphaFoldDB; A0A1Q5N793; -.
DR STRING; 1703927.AMK16_03930; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000185643; 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:OKK22314.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185643}.
FT DOMAIN 51..456
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 518..664
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ SEQUENCE 665 AA; 73464 MW; C88D54CB607731BC CRC64;
MSDTVNDYTR YTTGEPLVDT KAPDGPIAER WDRRRFEARL VNPANRRKHT VIVVGTGLAG
GAAGATLAEQ GYHVVQFCFS DSPRRAHSIA AQGGINAAKN YRNDGDSVHR LFYDTVKGGD
FRARESNVHR LAQISVEIID QCVAQGVPFA REYGGLLDTR SFGGVQVSRT FYARGQTGQQ
LLLGAYQALS RQIAAGGVEM HARTEMLDLI TVDGVARGIV ARDLVTGEVS THYADAVVLA
SGGYGNVFYL STNAMNSNAT AVWRAHRRGA YFANPCFTQI HPTCIPRTGD HQSKLTLMSE
SLRNDGRIWV PKAQGDTRPA ADIPEAERDY YLERIYPSFG NLVPRDIASR AAKNVCDEGR
GVGPGGQGVY LDFADAIRRM GRDKVAEKYG NLFEMYERIT AENPYEVPMR IYPAVHYTMG
GLWVDYDLQT TVPGLFAIGE ANFSDHGANR LGASALMQGL ADGYFVLPST INDYLARHPH
QDAIDDTHPE ARAALRDTRE RLARLLAVDG DRTPDSFHRE IGELMWEYCG MARTEEGLRT
ALARIPEIRE EFWRRVKVPG TGEEFNQSLE KANRIVDYLE LAELMCLDAL ARAESCGGHF
REESQTPDGE AERRDEEFSY VAAWEYRAPA SPPPGGGAGP AGAAPVLHKE DLVFEYVHPT
QRSYA
//
