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Database: UniProt
Entry: A0A101S5N6_9ACTN
LinkDB: A0A101S5N6_9ACTN
Original site: A0A101S5N6_9ACTN 
ID   A0A101S5N6_9ACTN        Unreviewed;       249 AA.
AC   A0A101S5N6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:KUN67939.1};
GN   ORFNames=AQJ54_12950 {ECO:0000313|EMBL:KUN67939.1};
OS   Streptomyces griseorubiginosus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67304 {ECO:0000313|EMBL:KUN67939.1, ECO:0000313|Proteomes:UP000054375};
RN   [1] {ECO:0000313|EMBL:KUN67939.1, ECO:0000313|Proteomes:UP000054375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40469 {ECO:0000313|EMBL:KUN67939.1,
RC   ECO:0000313|Proteomes:UP000054375};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces griseorubiginosus DSM 40469, type
RT   strain for the species Streptomyces griseorubiginosus.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|ARBA:ARBA00001927};
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC       iron-sulfur protein family. {ECO:0000256|ARBA:ARBA00009433}.
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:KUN67939.1}.
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DR   EMBL; LMWV01000007; KUN67939.1; -; Genomic_DNA.
DR   RefSeq; WP_062237219.1; NZ_KQ948736.1.
DR   AlphaFoldDB; A0A101S5N6; -.
DR   Proteomes; UP000054375; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR   PANTHER; PTHR11921:SF41; 4FE-4S FERREDOXIN IRON-SULFUR BINDING DOMAIN PROTEIN; 1.
DR   PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1.
DR   Pfam; PF13085; Fer2_3; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054375}.
FT   DOMAIN          1..102
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          149..178
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   249 AA;  26833 MW;  0259EBF84348BAAC CRC64;
     MKLTLRVWRQ KNADADGAMS TYEVDGISSD MSFLEMLDTL NEELILRGED PVAFDHDCRE
     GICGACSLVI NGDAHGPERT TTCQLHMRSF SDGDTIDIEP WRAAAFPVIK DLVVDRSAFD
     RIIQAGGYIT APTGAAPEAH ATPVPKPDAD FAFEHAECIG CGACVAACPN GAAMLFTSAK
     VNHLNVLPQG APERETRVLD MVEQMDEEGF GGCTLTGECA TACPKGIPLV SITSMNKEWL
     RATRKVGKR
//
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