ID E0W3X5_PEDHC Unreviewed; 292 AA.
AC E0W3X5;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 Name=8239726 {ECO:0000313|EnsemblMetazoa:PHUM612230-PA};
GN ORFNames=Phum_PHUM612230 {ECO:0000313|EMBL:EEB20331.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB20331.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB20331.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB20331.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB20331.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM612230-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM612230-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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;
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; fumarate
CC from succinate (eukaryal route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004788, ECO:0000256|RuleBase:RU361237}.
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}.
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DR EMBL; AAZO01007483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235883; EEB20331.1; -; Genomic_DNA.
DR RefSeq; XP_002433069.1; XM_002433024.1.
DR AlphaFoldDB; E0W3X5; -.
DR STRING; 121224.E0W3X5; -.
DR EnsemblMetazoa; PHUM612230-RA; PHUM612230-PA; PHUM612230.
DR GeneID; 8239726; -.
DR KEGG; phu:Phum_PHUM612230; -.
DR CTD; 8239726; -.
DR VEuPathDB; VectorBase:PHUM612230; -.
DR eggNOG; KOG3049; Eukaryota.
DR HOGENOM; CLU_044838_0_2_1; -.
DR InParanoid; E0W3X5; -.
DR OMA; MVMVRHA; -.
DR OrthoDB; 119960at2759; -.
DR UniPathway; UPA00223; UER01006.
DR Proteomes; UP000009046; 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 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 ECO:0000313|EMBL:EEB20331.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 44..135
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 178..208
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 292 AA; 33162 MW; F8AA2258A408D2E5 CRC64;
MVWEFVIRFR SLSPTYSSVR RLHSSKALLA AAREEVKEKS PQYKTFSIYR WDPDAVNEKP
RMQSYEVDLN SCGPMVLDAL IKIKNEIDPT LTFRRSCREG ICGSCAMNIG GVNTLACISK
ISQSGTTKIY PLPHMYVVKD LVPDMTNFYN QYKSIQPWLQ RKNEAEPGTE QYLQSVKDRD
VLDGLYECIL CACCSTSCPS YWWNGDKYLG PAALMQAYRW IIDSRDDNTK ERLSNLKDPF
SVFRCHTIMN CTKTCPKSLN PGKAIAELKK LLGGLASKPT PDLQPDALIK NK
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