ID A0A0B5DPZ9_9ACTN Unreviewed; 253 AA.
AC A0A0B5DPZ9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Succinate dehydrogenase iron-sulfur subunit {ECO:0000256|ARBA:ARBA00022131, ECO:0000256|RuleBase:RU361237};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792, ECO:0000256|RuleBase:RU361237};
GN ORFNames=BJY54_004014 {ECO:0000313|EMBL:MBB4793402.1}, CP978_20770
GN {ECO:0000313|EMBL:QEV40658.1}, SNOD_20440
GN {ECO:0000313|EMBL:AJE42142.1};
OS Streptomyces nodosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=40318 {ECO:0000313|EMBL:AJE42142.1, ECO:0000313|Proteomes:UP000031526};
RN [1] {ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526};
RA Sweeney P., Stephens N., Murphy C., Caffrey P.;
RT "Sequence of the Streptomyces nodosus genome.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJE42142.1, ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:AJE42142.1,
RC ECO:0000313|Proteomes:UP000031526};
RX PubMed=26497174;
RA Sweeney P., Murphy C.D., Caffrey P.;
RT "Exploiting the genome sequence of Streptomyces nodosus for enhanced
RT antibiotic production.";
RL Appl. Microbiol. Biotechnol. 100:1285-1295(2016).
RN [3] {ECO:0000313|EMBL:QEV40658.1, ECO:0000313|Proteomes:UP000325763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:QEV40658.1,
RC ECO:0000313|Proteomes:UP000325763};
RA Lee N., Cho B.-K.;
RT "Streptomyces genome completion.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:MBB4793402.1, ECO:0000313|Proteomes:UP000544950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40109 {ECO:0000313|EMBL:MBB4793402.1,
RC ECO:0000313|Proteomes:UP000544950};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361237};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|RuleBase:RU361237};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000256|RuleBase:RU361237};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|RuleBase:RU361237};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU361237};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237};
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,
CC ECO:0000256|RuleBase:RU361237}.
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DR EMBL; CP009313; AJE42142.1; -; Genomic_DNA.
DR EMBL; JACHMR010000001; MBB4793402.1; -; Genomic_DNA.
DR EMBL; CP023747; QEV40658.1; -; Genomic_DNA.
DR RefSeq; WP_043443236.1; NZ_JACHMR010000001.1.
DR STRING; 40318.SNOD_20440; -.
DR KEGG; snq:CP978_20770; -.
DR HOGENOM; CLU_044838_3_0_11; -.
DR OrthoDB; 9804391at2; -.
DR Proteomes; UP000031526; Chromosome.
DR Proteomes; UP000325763; Chromosome.
DR Proteomes; UP000544950; Unassembled WGS sequence.
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:0051539; F:4 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.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|RuleBase:RU361237};
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291, ECO:0000256|RuleBase:RU361237};
KW 4Fe-4S {ECO:0000256|RuleBase:RU361237};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361237};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361237};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361237};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:MBB4793402.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031526};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 19..113
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 155..177
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 253 AA; 28825 MW; 0A27E8045B0E606E CRC64;
MATPVLDKVE AQSAASPYIT VTFRIRRFNP EVSAESVWED FQLELDPKER VLDGLHKIKW
DLDGTLTFRR SCAHGICGSD AMRINGKNRL ACKTLIKDIN PEKPITVEPI KGLTVLKDLV
VDMEPFFQAY RDVMPFLITK GTNEPTRERL QSAEDRERFD DTTKCILCAA CTSSCPVFWN
DGQYFGPAAI VNAHRFIFDS RDEAGEQRLE ILNDKDGVWR CRTTFNCTDA CPRGIEVTKA
IQEVKRALIT RRF
//
