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Database: UniProt
Entry: A0A172TA33_9DEIO
LinkDB: A0A172TA33_9DEIO
Original site: A0A172TA33_9DEIO 
ID   A0A172TA33_9DEIO        Unreviewed;       253 AA.
AC   A0A172TA33;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Succinate dehydrogenase iron-sulfur subunit {ECO:0000256|ARBA:ARBA00022131};
DE            EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792};
GN   ORFNames=SU48_08590 {ECO:0000313|EMBL:ANE43822.1};
OS   Deinococcus puniceus.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=1182568 {ECO:0000313|EMBL:ANE43822.1, ECO:0000313|Proteomes:UP000077363};
RN   [1] {ECO:0000313|EMBL:ANE43822.1, ECO:0000313|Proteomes:UP000077363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY1 {ECO:0000313|EMBL:ANE43822.1,
RC   ECO:0000313|Proteomes:UP000077363};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Deinococcus puniceus/DY1/ whole genome sequencing.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000256|ARBA:ARBA00001927};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC       {ECO:0000256|ARBA:ARBA00005163}.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC       iron-sulfur protein family. {ECO:0000256|ARBA:ARBA00009433}.
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DR   EMBL; CP011387; ANE43822.1; -; Genomic_DNA.
DR   RefSeq; WP_064014891.1; NZ_CP011387.1.
DR   AlphaFoldDB; A0A172TA33; -.
DR   STRING; 1182568.SU48_08590; -.
DR   KEGG; dpu:SU48_08590; -.
DR   PATRIC; fig|1182568.3.peg.1785; -.
DR   OrthoDB; 9804391at2; -.
DR   Proteomes; UP000077363; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
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; 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; 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   Pfam; PF13237; Fer4_10; 1.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077363};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          20..112
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   253 AA;  28587 MW;  914E56C82CDDB7DD CRC64;
     MTQAQLTPST PATAAAMMTL KVKVLRFDPE KDKKAHWVTY EVEAQAADRV LDVINHVKWY
     MDPSLTFRRS CGHGICGSDA MLINGRNRLA CKTLLRDVVK KSGDTITVEP IRGLKVEKDL
     LVDMEPFFDS YKAIMPYFIN ESPEPAAERI QSPELAERMA HSSNCILCAC CTTSCPIFWV
     NGSYLGPASI VQAHRFIFDS RDEATQQRLN IMNQNTGVWR CRTAYNCTEA CPRDIPITQL
     IEEVKRAVMY QQS
//
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