ID A0A4T0RI67_9BASI Unreviewed; 286 AA.
AC A0A4T0RI67;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial {ECO:0000256|ARBA:ARBA00016766, ECO:0000256|RuleBase:RU361237};
DE EC=1.3.5.1 {ECO:0000256|ARBA:ARBA00012792, ECO:0000256|RuleBase:RU361237};
GN ORFNames=E3Q01_04003 {ECO:0000313|EMBL:TIC62325.1}, E3Q09_03959
GN {ECO:0000313|EMBL:TIC31773.1}, E3Q10_04066
GN {ECO:0000313|EMBL:TIC24453.1}, E3Q13_04080
GN {ECO:0000313|EMBL:TIC12817.1}, E3Q17_03946
GN {ECO:0000313|EMBL:TIB96241.1}, E3Q18_04097
GN {ECO:0000313|EMBL:TIB94957.1}, E3Q22_04011
GN {ECO:0000313|EMBL:TIB75436.1};
OS Wallemia mellicola.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1708541 {ECO:0000313|EMBL:TIC62325.1, ECO:0000313|Proteomes:UP000310708};
RN [1] {ECO:0000313|Proteomes:UP000305647, ECO:0000313|Proteomes:UP000307169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-1262 {ECO:0000313|EMBL:TIB96241.1,
RC ECO:0000313|Proteomes:UP000307169}, EXF-1443
RC {ECO:0000313|EMBL:TIB94957.1, ECO:0000313|Proteomes:UP000308061},
RC EXF-6152 {ECO:0000313|EMBL:TIB75436.1,
RC ECO:0000313|Proteomes:UP000310685}, EXF-6158
RC {ECO:0000313|EMBL:TIC31773.1, ECO:0000313|Proteomes:UP000308095},
RC EXF-757 {ECO:0000313|EMBL:TIC62325.1,
RC ECO:0000313|Proteomes:UP000310708}, EXF-8738
RC {ECO:0000313|EMBL:TIC24453.1, ECO:0000313|Proteomes:UP000305647}, and
RC EXF-8749 {ECO:0000313|EMBL:TIC12817.1,
RC ECO:0000313|Proteomes:UP000310225};
RA Gostincar C.;
RT "Sequencing 25 genomes of Wallemia mellicola.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Iron-sulfur protein (IP) subunit of succinate dehydrogenase
CC (SDH) that is involved in complex II of the mitochondrial electron
CC transport chain and is responsible for transferring electrons from
CC succinate to ubiquinone (coenzyme Q). {ECO:0000256|RuleBase:RU361237}.
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=[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; fumarate
CC from succinate (eukaryal route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004788, ECO:0000256|RuleBase:RU361237}.
CC -!- SUBUNIT: Component of complex II composed of four subunits: a
CC flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b
CC composed of a large and a small subunit.
CC {ECO:0000256|ARBA:ARBA00011421}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU361237};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443,
CC ECO:0000256|RuleBase:RU361237}; Matrix side
CC {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU361237}.
CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase
CC iron-sulfur protein family. {ECO:0000256|ARBA:ARBA00009433,
CC ECO:0000256|RuleBase:RU361237}.
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:TIC62325.1}.
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DR EMBL; SPRC01000064; TIB75436.1; -; Genomic_DNA.
DR EMBL; SPRG01000070; TIB94957.1; -; Genomic_DNA.
DR EMBL; SPRH01000068; TIB96241.1; -; Genomic_DNA.
DR EMBL; SPRL01000062; TIC12817.1; -; Genomic_DNA.
DR EMBL; SPRO01000071; TIC24453.1; -; Genomic_DNA.
DR EMBL; SPRP01000062; TIC31773.1; -; Genomic_DNA.
DR EMBL; SPRX01000072; TIC62325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4T0RI67; -.
DR UniPathway; UPA00223; UER01006.
DR Proteomes; UP000305647; Unassembled WGS sequence.
DR Proteomes; UP000307169; Unassembled WGS sequence.
DR Proteomes; UP000308061; Unassembled WGS sequence.
DR Proteomes; UP000308095; Unassembled WGS sequence.
DR Proteomes; UP000310225; Unassembled WGS sequence.
DR Proteomes; UP000310685; Unassembled WGS sequence.
DR Proteomes; UP000310708; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; 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; 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; PF13534; Fer4_17; 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 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|RuleBase:RU361237};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361237};
KW Membrane {ECO:0000256|RuleBase:RU361237};
KW Metal-binding {ECO:0000256|RuleBase:RU361237};
KW Mitochondrion {ECO:0000256|RuleBase:RU361237};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU361237};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000310685};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 57..148
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 189..219
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 286 AA; 32567 MW; 1FED4DB24DE1E049 CRC64;
MQSDLSKSRF NSTIIIKMLN LGKSALPVNG AMRSFSTSTR RALATPVGAK PPHMKKFQIY
RWNPDKPAEK PRMQTYDVDL NACGPMVLDA LLKIKNEADP TLTFRRSCRE GICGSCAMNI
EGQNTLACLC RIDRNENKAS KIYPLPHMYI VKDLVPDMTQ FYKQYKSIEP YLQSDNVPDG
VEHRQSPEER KKLDGMYECI LCACCSTSCP SYWWNQDEYL GPAVLMQAYR WIADSRDSKA
AERKEKLENT FSLYRCHTIF NCTRTCPKGL NPAKAIAEMK KEMATA
//
