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Protein

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Gene

SDH2

Organism
Zymoseptoria tritici (Speckled leaf blotch fungus) (Septoria tritici)
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:

Pathwayi: tricarboxylic 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 (SdhB), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SdhB), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SdhB), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SdhB), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SdhB), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SDH2), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SdhB), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SdhB), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SdhB), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SdhB), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (SdhB)
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)DescriptionActionsGraphical viewLength
Metal bindingi117Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi122Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi125Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi137Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi209Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi212Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi215Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi219Iron-sulfur 3 (3Fe-4S)By similarity1
Binding sitei224Ubiquinone; shared with DHSDBy similarity1
Metal bindingi266Iron-sulfur 3 (3Fe-4S)By similarity1
Metal bindingi272Iron-sulfur 3 (3Fe-4S)By similarity1
Metal bindingi276Iron-sulfur 2 (4Fe-4S)By similarity1

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
OrganismiZymoseptoria tritici (Speckled leaf blotch fungus) (Septoria tritici)
Taxonomic identifieri1047171 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesDothideomycetidaeCapnodialesMycosphaerellaceaeZymoseptoria

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL613815.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000010349? – 297Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

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

Chemistry databases

BindingDBiO42772.

Structurei

3D structure databases

ProteinModelPortaliO42772.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini78 – 1572Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST80
Domaini199 – 2294Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd BLAST31

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

OMAiDGQYFGP.

Family and domain databases

CDDicd00207. fer2. 1 hit.
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.

O42772-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRLATRRF APIAFRRGMA TTIEHTKEPI SATAEALSAS RPPIKETKTS
60 70 80 90 100
TVKEPQMDAD AKTKTFHIYR WNPDQPTDKP RMQSYTLDLN KTGPMMLDAL
110 120 130 140 150
IRIKNEVDPT LTFRRSCREG ICGSCAMNID GVNTLACLCR IPTDTAKETR
160 170 180 190 200
IYPLPHTYVV KDLVPDMTQF YKQYKSIKPY LQRDTAPPDG KENRQSVADR
210 220 230 240 250
KKLDGLYECI LCACCSTSCP SYWWNSEEYL GPAVLLQSYR WINDSRDEKT
260 270 280 290
AQRKDALNNS MSLYRCHTIL NCSRTCPKGL NPALAIAEIK KSMAFTG
Length:297
Mass (Da):33,667
Last modified:June 1, 1998 - v1
Checksum:iA50010A24F48F6D4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042062 Genomic DNA. Translation: AAB97419.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042062 Genomic DNA. Translation: AAB97419.1.

3D structure databases

ProteinModelPortaliO42772.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiO42772.
ChEMBLiCHEMBL613815.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OMAiDGQYFGP.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.

Family and domain databases

CDDicd00207. fer2. 1 hit.
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...

Entry informationi

Entry nameiSDHB_ZYMTR
AccessioniPrimary (citable) accession number: O42772
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 1, 1998
Last modified: October 5, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

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

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 one 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.