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Database: UniProt
Entry: A0A0W7W880_9MICO
LinkDB: A0A0W7W880_9MICO
Original site: A0A0W7W880_9MICO 
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
//
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