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Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Gene

SDH2

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

Protein has several cofactor binding sites:

Pathway:itricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes fumarate from succinate (eukaryal route).
Proteins known to be involved in this subpathway in this organism are:
  1. Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SDH2), Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (AGOS_ACR052W)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes fumarate from succinate (eukaryal route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi82 – 821Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi87 – 871Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi90 – 901Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi102 – 1021Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi174 – 1741Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi177 – 1771Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi180 – 1801Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi184 – 1841Iron-sulfur 3 (3Fe-4S)By similarity
Binding sitei189 – 1891Ubiquinone; shared with DHSDBy similarity
Metal bindingi231 – 2311Iron-sulfur 3 (3Fe-4S)By similarity
Metal bindingi237 – 2371Iron-sulfur 3 (3Fe-4S)By similarity
Metal bindingi241 – 2411Iron-sulfur 2 (4Fe-4S)By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

2Fe-2S, 3Fe-4S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (EC:1.3.5.1)
Alternative name(s):
Iron-sulfur subunit of complex II
Short name:
Ip
Gene namesi
Name:SDH2
Ordered Locus Names:ACL065C
OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Taxonomic identifieri284811 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
ProteomesiUP000000591 Componenti: Chromosome III

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 261Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialPRO_0000010347
Transit peptidei1 – ?Mitochondrion

Proteomic databases

PRIDEiQ75CI4.

Interactioni

Subunit structurei

Component of complex II composed of four subunits: a flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a large and a small subunit.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ75CI4.
SMRiQ75CI4. Positions 24-259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 122922Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini164 – 194314Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0479.
HOGENOMiHOG000160590.
InParanoidiQ75CI4.
KOiK00235.
OMAiIQVTQAI.
OrthoDBiEOG7X9GJ0.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamiPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q75CI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVFRAGIGRI GLIRGLATQA AEVSATRYKS FKIYRWNPDT PAEKPRMQEY
60 70 80 90 100
KVDLNKCGPM VLDALIKIKN EQDPTLTFRR SCREGICGSC AMNIGGRNTL
110 120 130 140 150
ACLCKIDQAE NKDVKIYPLP HMYVVKDLVP DLTNFYKQYK SIQPYLQKAS
160 170 180 190 200
KPADGREHLQ SIADRKKLDG LYECILCACC STACPSYWWN NEQYLGPAVL
210 220 230 240 250
MQAYRWMVDS RDGAGAGRRE QLQNAMSVYR CHTIMNCTRT CPKGLNPGKA
260
IAEIKKALAF A
Length:261
Mass (Da):29,436
Last modified:July 5, 2004 - v1
Checksum:i7F11084887FC7F5A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016816 Genomic DNA. Translation: AAS51163.1.
RefSeqiNP_983339.1. NM_208692.1.

Genome annotation databases

EnsemblFungiiAAS51163; AAS51163; AGOS_ACL065C.
GeneIDi4619459.
KEGGiago:AGOS_ACL065C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016816 Genomic DNA. Translation: AAS51163.1.
RefSeqiNP_983339.1. NM_208692.1.

3D structure databases

ProteinModelPortaliQ75CI4.
SMRiQ75CI4. Positions 24-259.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ75CI4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiAAS51163; AAS51163; AGOS_ACL065C.
GeneIDi4619459.
KEGGiago:AGOS_ACL065C.

Phylogenomic databases

eggNOGiCOG0479.
HOGENOMiHOG000160590.
InParanoidiQ75CI4.
KOiK00235.
OMAiIQVTQAI.
OrthoDBiEOG7X9GJ0.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamiPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMiSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR00384. dhsB. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
    Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
    Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
  2. "Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
    Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
    G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Entry informationi

Entry nameiSDHB_ASHGO
AccessioniPrimary (citable) accession number: Q75CI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 5, 2004
Last modified: July 22, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.