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Database: UniProt
Entry: A0A087SSZ1_AUXPR
LinkDB: A0A087SSZ1_AUXPR
Original site: A0A087SSZ1_AUXPR 
ID   A0A087SSZ1_AUXPR        Unreviewed;       275 AA.
AC   A0A087SSZ1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial {ECO:0000256|RuleBase:RU361237};
DE            EC=1.3.5.1 {ECO:0000256|RuleBase:RU361237};
GN   ORFNames=APUTEX25_003221 {ECO:0000313|EMBL:RMZ53687.1}, F751_4320
GN   {ECO:0000313|EMBL:KFM28845.1};
OS   Auxenochlorella protothecoides (Green microalga) (Chlorella
OS   protothecoides).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Auxenochlorella.
OX   NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM28845.1, ECO:0000313|Proteomes:UP000028924};
RN   [1] {ECO:0000313|EMBL:KFM28845.1, ECO:0000313|Proteomes:UP000028924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0710 {ECO:0000313|EMBL:KFM28845.1,
RC   ECO:0000313|Proteomes:UP000028924};
RX   PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA   Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT   "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT   protothecoides revealed through its genome, transcriptomes, and
RT   proteomes.";
RL   BMC Genomics 15:582-582(2014).
RN   [2] {ECO:0000313|Proteomes:UP000279271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 25 {ECO:0000313|Proteomes:UP000279271};
RX   DOI=10.1016/j.algal.2018.07.001;
RA   Vogler B.W., Starkenburg S.R., Sudasinghe N., Schambach J.Y., Rollin J.A.,
RA   Pattathil S., Barry A.N.;
RT   "Characterization of plant carbon substrate utilization by Auxenochlorella
RT   protothecoides.";
RL   Algal Res. 34:37-48(2018).
RN   [3] {ECO:0000313|EMBL:RMZ53687.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 25 {ECO:0000313|EMBL:RMZ53687.1};
RA   Hovde B., Zhang X.;
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:RMZ53687.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 25 {ECO:0000313|EMBL:RMZ53687.1};
RA   Vogler B.W., Starkenburg S.R., Sudasinghe N., Schambach J.Y., Rollin J.A.,
RA   Pattathil S., Barry A.N.;
RT   "Characterization of plant carbon substrate utilization by Auxenochlorella
RT   protothecoides.";
RL   Submitted (NOV-2018) 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|ARBA:ARBA00002787,
CC       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   -!- SUBUNIT: Component of complex II composed of eight subunits in plants:
CC       four classical SDH subunits SDH1, SDH2, SDH3 and SDH4 (a flavoprotein
CC       (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a
CC       large and a small subunit.), as well as four subunits unknown in
CC       mitochondria from bacteria and heterotrophic eukaryotes.
CC       {ECO:0000256|ARBA:ARBA00011313}.
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; KL662183; KFM28845.1; -; Genomic_DNA.
DR   EMBL; QOKY01000196; RMZ53687.1; -; Genomic_DNA.
DR   RefSeq; XP_011401894.1; XM_011403592.1.
DR   STRING; 3075.A0A087SSZ1; -.
DR   GeneID; 23615711; -.
DR   KEGG; apro:F751_4320; -.
DR   eggNOG; KOG3049; Eukaryota.
DR   OrthoDB; 119960at2759; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000028924; Unassembled WGS sequence.
DR   Proteomes; UP000279271; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045273; C:respiratory chain complex II; IEA:UniProt.
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; PF13183; Fer4_8; 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|ARBA:ARBA00023004, 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:UP000028924};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532};
KW   Ubiquinone {ECO:0000313|EMBL:KFM28845.1}.
FT   DOMAIN          45..131
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          175..205
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   275 AA;  30320 MW;  5FC290241123CDA9 CRC64;
     MLSLSRALAR GAARAAPEIG FVRAAATSAA TPAAAAKPVV EKEFLVYRWN PDDGEAPKYQ
     TYKVDINSCG PMMLDVLLKI KDDHDSSLSL RRSCREGICG SCAMNIDGKN GLACLTKVER
     DPSAVTRVAP LPHMFVIRDL VVDMANFYAQ YKSIKPFLLK PKPADGLEHR QTKEDRAKLD
     GLYECILCAC CSTSCPSYWW NSDKYLGPAV LLQAYRWVID SRDEATTQRL ADLDDQFKLY
     RCKTIMNCAT VCPKGLNPGK AIAKIKQSVA AGRAF
//
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