Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P32420 (SDHB_USTMA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Synonyms:CBXR
OrganismUstilago maydis (strain 521 / FGSC 9021) (Corn smut fungus) [Reference proteome]
Taxonomic identifier237631 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaUstilaginomycotinaUstilaginomycetesUstilaginalesUstilaginaceaeUstilago

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 295Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrialPRO_0000010352

Regions

Domain67 – 144782Fe-2S ferredoxin-type
Domain185 – 215314Fe-4S ferredoxin-type

Sites

Metal binding1061Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1111Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1141Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1261Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1951Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1981Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2011Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding2051Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2521Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2581Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2621Iron-sulfur 2 (4Fe-4S) By similarity
Binding site2101Ubiquinone; shared with DHSD By similarity

Natural variations

Natural variant2531H → L in carboxin-resistant mutant.

Sequences

Sequence LengthMass (Da)Tools
P32420 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: F374A20BA8F8E7E5

FASTA29533,282
        10         20         30         40         50         60 
MSLFNVSNGL RTALRPSVAS SSRVAAFSTT AAARLATPTS DNVGSSGKPQ HLKQFKIYRW 

        70         80         90        100        110        120 
NPDKPSEKPR LQSYTLDLNQ TGPMVLDALI KIKNEIDPTL TFRRSCREGI CGSCAMNIDG 

       130        140        150        160        170        180 
VNTLACLCRI DKQNDTKIYP LPHMYIVKDL VPDLTQFYKQ YRSIEPFLKS NNTPSEGEHL 

       190        200        210        220        230        240 
QSPEERRRLD GLYECILCAC CSTSCPSYWW NQDEYLGPAV LMQAYRWMAD SRDDFGEERR 

       250        260        270        280        290 
QKLENTFSLY RCHTIMNCSR TCPKNLNPGK AIAQIKKDMA VGAPKASERP IMASS 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, characterization and sequence of a gene conferring resistance to the systemic fungicide carboxin from the maize smut pathogen, Ustilago maydis."
Keon J.P.R., White G.A., Hargreaves J.A.
Curr. Genet. 19:475-481(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 38509 / 92.
[2]"A single amino-acid change in the iron-sulphur protein subunit of succinate dehydrogenase confers resistance to carboxin in Ustilago maydis."
Broomfield P.L.E., Hargreaves J.A.
Curr. Genet. 22:117-121(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis."
Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J. expand/collapse author list , Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L., Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.
Nature 444:97-101(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 521 / FGSC 9021.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X62762 Genomic DNA. Translation: CAA44612.1.
Z11738 Genomic DNA. Translation: CAA77798.1.
AACP01000027 Genomic DNA. Translation: EAK81918.1.
PIRS26978.
RefSeqXP_756991.1. XM_751898.1.

3D structure databases

ProteinModelPortalP32420.
SMRP32420. Positions 52-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5270.UM00844.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiUM00844T0; UM00844P0; UM00844.
GeneID3628909.
KEGGuma:UM00844.1.

Phylogenomic databases

eggNOGCOG0479.
HOGENOMHOG000160590.
KOK00235.
OMADSHERML.
OrthoDBEOG7X9GJ0.

Enzyme and pathway databases

UniPathwayUPA00223; UER01006.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 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]
PfamPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR00384. dhsB. 1 hit.
PROSITEPS00197. 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]
ProtoNetSearch...

Entry information

Entry nameSDHB_USTMA
AccessionPrimary (citable) accession number: P32420
Secondary accession number(s): Q12722, Q4PGB9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: March 19, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways