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Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (EC 1.3.5.1)

 A0A1P8BFU4_ARATH        Unreviewed;       224 AA.
A0A1P8BFU4;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
05-DEC-2018, entry version 12.
RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial {ECO:0000256|RuleBase:RU361237};
EC=1.3.5.1 {ECO:0000256|RuleBase:RU361237};
Name=SDH2-2 {ECO:0000313|EMBL:ANM70488.1};
Synonyms=MNF13.170 {ECO:0000313|EMBL:ANM70488.1},
MNF13_170 {ECO:0000313|EMBL:ANM70488.1},
succinate dehydrogenase 2-2 {ECO:0000313|EMBL:ANM70488.1};
OrderedLocusNames=At5g40650 {ECO:0000313|EMBL:ANM70488.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000313|EMBL:ANM70488.1, ECO:0000313|Proteomes:UP000006548};
[1] {ECO:0000313|EMBL:ANM70488.1, ECO:0000313|Proteomes:UP000006548}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
PubMed=11130714; DOI=10.1038/35048507;
Kazusa DNA Research Institute;
Cold Spring Harbor and Washington University in St Louis Sequencing Consortium;
European Union Arabidopsis Genome Sequencing Consortium;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., See L.H., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T.,
Entian K.D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.A.,
McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Lankhorst R.K., Weitzenegger T., Bothe G., Rose M.,
Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
Mayer K., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.W.,
Bevan M., Fransz P.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[2] {ECO:0000313|Proteomes:UP000006548}
GENOME REANNOTATION.
STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
-!- FUNCTION: Iron-sulfur protein (IP) subunit of succinate
dehydrogenase (SDH) that is involved in complex II of the
mitochondrial electron transport chain and is responsible for
transferring electrons from succinate to ubiquinone (coenzyme Q).
{ECO:0000256|RuleBase:RU361237}.
-!- CATALYTIC ACTIVITY:
Reaction=a quinone + succinate = a quinol + fumarate;
Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
Evidence={ECO:0000256|RuleBase:RU361237};
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000256|RuleBase:RU361237};
Note=Binds 1 [2Fe-2S] cluster. {ECO:0000256|RuleBase:RU361237};
-!- COFACTOR:
Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
Evidence={ECO:0000256|RuleBase:RU361237};
Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237};
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000256|RuleBase:RU361237};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|RuleBase:RU361237};
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
fumarate from succinate (eukaryal route): step 1/1.
{ECO:0000256|RuleBase:RU361237}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000256|RuleBase:RU361237}; Peripheral membrane protein
{ECO:0000256|RuleBase:RU361237}; Matrix side
{ECO:0000256|RuleBase:RU361237}.
-!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
reductase iron-sulfur protein family.
{ECO:0000256|RuleBase:RU361237}.
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EMBL; CP002688; ANM70488.1; -; Genomic_DNA.
RefSeq; NP_001332094.1; NM_001344348.1.
UniGene; At.20145; -.
UniGene; At.67187; -.
UniGene; At.7421; -.
SMR; A0A1P8BFU4; -.
EnsemblPlants; AT5G40650.2; AT5G40650.2; AT5G40650.
GeneID; 834065; -.
Gramene; AT5G40650.2; AT5G40650.2; AT5G40650.
OMA; KHIAHIK; -.
UniPathway; UPA00223; UER01006.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; A0A1P8BFU4; baseline and differential.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
CDD; cd00207; fer2; 1.
Gene3D; 1.10.1060.10; -; 1.
Gene3D; 3.10.20.30; -; 1.
InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
InterPro; IPR006058; 2Fe2S_fd_BS.
InterPro; IPR017896; 4Fe4S_Fe-S-bd.
InterPro; IPR017900; 4Fe4S_Fe_S_CS.
InterPro; IPR012675; Beta-grasp_dom_sf.
InterPro; IPR009051; Helical_ferredxn.
InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S.
InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
Pfam; PF13085; Fer2_3; 1.
SUPFAM; SSF46548; SSF46548; 1.
SUPFAM; SSF54292; SSF54292; 1.
TIGRFAMs; TIGR00384; dhsB; 1.
PROSITE; PS00197; 2FE2S_FER_1; 1.
PROSITE; PS51085; 2FE2S_FER_2; 1.
PROSITE; PS00198; 4FE4S_FER_1; 1.
PROSITE; PS51379; 4FE4S_FER_2; 1.
3: Inferred from homology;
2Fe-2S {ECO:0000256|RuleBase:RU361237};
3Fe-4S {ECO:0000256|RuleBase:RU361237};
4Fe-4S {ECO:0000256|RuleBase:RU361237};
Complete proteome {ECO:0000313|Proteomes:UP000006548};
Iron {ECO:0000256|RuleBase:RU361237};
Iron-sulfur {ECO:0000256|RuleBase:RU361237};
Membrane {ECO:0000256|RuleBase:RU361237};
Metal-binding {ECO:0000256|RuleBase:RU361237};
Mitochondrion {ECO:0000256|RuleBase:RU361237};
Mitochondrion inner membrane {ECO:0000256|RuleBase:RU361237};
Reference proteome {ECO:0000313|Proteomes:UP000006548}.
DOMAIN 51 140 2Fe-2S ferredoxin-type.
{ECO:0000259|PROSITE:PS51085}.
DOMAIN 183 213 4Fe-4S ferredoxin-type.
{ECO:0000259|PROSITE:PS51379}.
SEQUENCE 224 AA; 24639 MW; 4D4A9AA00735E49B CRC64;
MAFGLIGRVV GTKSSRLSTA ARLIPARWTS TGSEAQSKAS TGGGGASLKT FQIYRWNPDN
PGKPELQDYK IDLKDCGPMV LDALIKIKNE MDPSLTFRRS CREGICGSCA MNIDGCNGLA
CLTKIESGSK ETTITPLPHM FVIKDLVVDM TNFYNQYKSI EPWLKRKNPA SVPGKEILQS
KKDRAKLDGM YECILCACCS TSCPSYWWNP ESYLGPAALL HANR


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