ID A0A0W7W880_9MICO Unreviewed; 582 AA.
AC A0A0W7W880;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:KUF06711.1};
GN ORFNames=AUL38_11855 {ECO:0000313|EMBL:KUF06711.1};
OS Leucobacter sp. G161.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=663704 {ECO:0000313|EMBL:KUF06711.1, ECO:0000313|Proteomes:UP000053012};
RN [1] {ECO:0000313|EMBL:KUF06711.1, ECO:0000313|Proteomes:UP000053012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G161 {ECO:0000313|EMBL:KUF06711.1,
RC ECO:0000313|Proteomes:UP000053012};
RA Ge S., Dong X.;
RT "High quality draft genome sequence of Leucobacter sp. G161, a distinct and
RT effective chromium reducer.";
RL Submitted (DEC-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:KUF06711.1}.
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DR EMBL; LOHP01000064; KUF06711.1; -; Genomic_DNA.
DR RefSeq; WP_059061916.1; NZ_LOHP01000064.1.
DR AlphaFoldDB; A0A0W7W880; -.
DR STRING; 663704.AUL38_11855; -.
DR OrthoDB; 9805351at2; -.
DR Proteomes; UP000053012; Unassembled WGS sequence.
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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR11632; SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT; 1.
DR PANTHER; PTHR11632:SF89; SUCCINATE DEHYDROGENASE [IRON-SULFUR SUBUNIT] (SUCCINIC DEHYDROGENASE)-RELATED; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 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 Reference proteome {ECO:0000313|Proteomes:UP000053012}.
FT DOMAIN 15..395
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 450..539
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 582 AA; 63014 MW; DA08C4799FEF592A CRC64;
MTATRTQERL ISTSALVIGT GGAGLRASIE LAERGVQVLA VGKRRKHDAH TTLAAGGINA
ALGMMDPEDS WEQHAADTLR ESYFLADPHI VEIVAKNAAR GIEDLERWGM PFAREADGRI
SQRFFGAHLY RRTCYAGDYT GLEIQRTLLR RAQELQVPIN DSIYITRLLV SDGRVFGAYG
FDIVDGTPVV IHADAVILAA GGHTRIWRNT SSRRDENTGD SFRLAALAGA RIRDAELVQF
HPSGILEPAD AAGLLVSEAA RGEGGILRNA LGERFMEKYD PERMELSTRD RVALASYTEI
TEGRGTANGG VFLDVSHLPR EQILEKLPRV YRNLIDLQML DITQSPIEIA PTAHYSMGGV
WVSAEEHATG VDGLYAIGEA ASGLHGANRL GGNSLIELLV YGRLTGGDAA DYITGLSAIR
RDPHAVAAAR AEMQGLLTGT GEESPRLLQR QLRNVMTEHA GVVRSEAGLT EGLAKLDALA
ERVDNLTAHP DIAGFDDLAH AFDLYGSMLA ARATLESARE RRETRGAHNR SDFPEQCDEL
RGNMVWTPDG GVVFEPANAA PESFRALAEQ GIDDSPVGKL AE
//