Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot Q75CI4 (DHSB_ASHGO)

Last modified February 9, 2010. Version 51. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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 names

Name:	SDH2
Ordered Locus Names:	ACL065C

Organism

Ashbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]

Taxonomic identifier

33169 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium

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Protein attributes

Sequence length	261 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

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General annotation (Comments)

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) By similarity.
Catalytic activity	Succinate + ubiquinone = fumarate + ubiquinol.
Cofactor	Binds 1 2Fe-2S cluster By similarity. Binds 1 3Fe-4S cluster By similarity. Binds 1 4Fe-4S cluster By similarity.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (eukaryal route): step 1/1.
Subunit structure	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.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity.
Sequence similarities	Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 4Fe-4S ferredoxin-type domain.

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Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW succinate dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion

Chain

? – 261

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

PRO_0000010347

Regions

Domain

31 – 122

2Fe-2S ferredoxin-type

Domain

164 – 194

4Fe-4S ferredoxin-type

Sites

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

102

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

174

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

177

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

180

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

184

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

231

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

237

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

241

Iron-sulfur 2 (4Fe-4S) By similarity

Binding site

189

Ubiquinone; shared with DHSD By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q75CI4-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 7F11084887FC7F5A
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FASTA

261

29,436

        10         20         30         40         50         60 
MVFRAGIGRI GLIRGLATQA AEVSATRYKS FKIYRWNPDT PAEKPRMQEY KVDLNKCGPM 

        70         80         90        100        110        120 
VLDALIKIKN EQDPTLTFRR SCREGICGSC AMNIGGRNTL ACLCKIDQAE NKDVKIYPLP 

       130        140        150        160        170        180 
HMYVVKDLVP DLTNFYKQYK SIQPYLQKAS KPADGREHLQ SIADRKKLDG LYECILCACC 

       190        200        210        220        230        240 
STACPSYWWN NEQYLGPAVL MQAYRWMVDS RDGAGAGRRE QLQNAMSVYR CHTIMNCTRT 

       250        260 
CPKGLNPGKA IAEIKKALAF A

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References

[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: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016816 Genomic DNA. Translation: AAS51163.1.
RefSeq	NP_983339.1.
3D structure databases
SMR	Q75CI4. Positions 24-259.
ModBase	Search...
Protein-protein interaction databases
STRING	Q75CI4.
Genome annotation databases
GeneID	4619459.
GenomeReviews	Gene locus ACL065C in contig AE016816_GR.
KEGG	ago:AGOS_ACL065C.
NMPDR	fig\|33169.1.peg.984.
Organism-specific databases
AGD	ACL065C.
Phylogenomic databases
eggNOG	fuNOG06803.
HOGENOM	HBG616382.
OMA	SLIAERH.
OrthoDB	EOG9BZPK2.
Enzyme and pathway databases
BRENDA	1.3.5.1. 279361.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. IPR012285. Fum_reductase_C. IPR009051. Helical_ferredxn. IPR004489. Succ_DH/fum_Rdtase_Fe-S. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
TIGRFAMs	TIGR00384. dhsB. 1 hit.
PROSITE	PS00197. 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]
ProtoNet	Search...

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Entry information

Entry name

DHSB_ASHGO

Accession

Primary (citable) accession number: Q75CI4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	July 5, 2004
Last modified:	February 9, 2010
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents