ID D7B6N2_NOCDD Unreviewed; 648 AA.
AC D7B6N2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Succinate dehydrogenase or fumarate reductase, flavoprotein subunit {ECO:0000313|EMBL:ADH69319.1};
DE EC=1.3.99.1 {ECO:0000313|EMBL:ADH69319.1};
GN OrderedLocusNames=Ndas_3922 {ECO:0000313|EMBL:ADH69319.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH69319.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH69319.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
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DR EMBL; CP002040; ADH69319.1; -; Genomic_DNA.
DR RefSeq; WP_013154926.1; NC_014210.1.
DR AlphaFoldDB; D7B6N2; -.
DR STRING; 446468.Ndas_3922; -.
DR KEGG; nda:Ndas_3922; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_014312_7_0_11; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000002219; Chromosome 1.
DR GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
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:ADH69319.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002219}.
FT DOMAIN 47..452
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 513..647
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 341
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630664-50"
SQ SEQUENCE 648 AA; 72025 MW; 322B2DCB36451936 CRC64;
MSDNDFYRVG DPIRDEKAPE GPINERWDKR RFSAKLVNPA NRRKLSVIMV GTGLAGASAA
ATLGEAGYKV TSFCYQDSPR RAHSIAAQGG INAAKNYRND GDSIYRLFYD TVKGGDFRSR
ESNVYRLAQT SVEIIDQCVA QGVPFAREYG GLLDNRSFGG VQVSRTFYAR GQTGQQLLIG
AYQALERQIA AGSVKMHTRH EMLEVIVVDG RARGVIVRDM VTGEIETHFA DAVVLATGGY
GNVFFLSTNA MGSNVTATWR AHRKGALFAN PCYTQIHPTC IPVSGDYQSK LTLMSESLRN
DGRIWVPKAH GDTRDPRQIP EEERDYYLER IYPAFGNLVP RDIASRAAKN VCDEGRGVGP
GGLGVYLDFA DAIARMGQDA VEAKYGNLFD MYQRITGENP YEVPMRIYPA VHYTMGGLWV
DYDLQSSIPG LFVTGEANFS DHGANRLGAS ALMQGLADGY FVLPNTINDY LSSGPFEALD
ESHPEAVAAK EQVTSRIDKL LSVQGSRTVD SFHKELGHIM WEYCGMERSE EGLTKAIELI
RALRAEFWRD VKVLGTNEEF NQALEKANRV ADFLELGELM CIDALHRRES CGGHFRAESQ
TEDGEALRHD DEFAYVAAWA FGGDDSKPVL HKEALEYEYV EMKQRSYK
//
