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Database: UniProt
Entry: Q2NSQ3_SODGM
LinkDB: Q2NSQ3_SODGM
Original site: Q2NSQ3_SODGM 
ID   Q2NSQ3_SODGM            Unreviewed;       150 AA.
AC   Q2NSQ3;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Fumarate reductase iron-sulfur protein subunit {ECO:0000313|EMBL:BAE74822.1};
GN   OrderedLocusNames=SG1547 {ECO:0000313|EMBL:BAE74822.1};
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509 {ECO:0000313|EMBL:BAE74822.1, ECO:0000313|Proteomes:UP000001932};
RN   [1] {ECO:0000313|EMBL:BAE74822.1, ECO:0000313|Proteomes:UP000001932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans {ECO:0000313|Proteomes:UP000001932};
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + succinate = a quinol + fumarate;
CC         Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000030};
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}.
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DR   EMBL; AP008232; BAE74822.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2NSQ3; -.
DR   STRING; 343509.SG1547; -.
DR   KEGG; sgl:SG1547; -.
DR   eggNOG; COG0479; Bacteria.
DR   HOGENOM; CLU_1739321_0_0_6; -.
DR   Proteomes; UP000001932; Chromosome.
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:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S.
DR   InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR   NCBIfam; TIGR00384; dhsB; 1.
DR   PANTHER; PTHR11921:SF29; SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1.
DR   Pfam; PF13085; Fer2_3; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
PE   3: Inferred from homology;
FT   DOMAIN          8..85
FT                   /note="Succinate dehydogenase/fumarate reductase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13085"
SQ   SEQUENCE   150 AA;  16795 MW;  0865DE596742001E CRC64;
     MADKHPLTVQ IQRYDPEKDR APQWESYPVP WDEQTSLLDA LGYIKDHLAA DLTFRWSCRM
     AICGSCGMMV NDVPRLTCKT FLSGFPARPE GAGAGEFPYR ARSGGGYERL YGNFIGHPAL
     DYWQQPHAGT GRQRATAHAN GEIPSICRLH
//
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