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

P47052 (SDHX_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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] flavoprotein subunit 2, mitochondrial

EC=1.3.5.1
Alternative name(s):
Flavoprotein subunit of complex II
Short name=FP
SDH1b
Gene names
Ordered Locus Names:YJL045W
ORF Names:J1194
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length634 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable minor catalytic 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). Probably forms a catalytic dimer with SDH2. Electrons flow from succinate to the FAD bound to the catalytic subunit, and sequentially through the iron-sulfur clusters bound to SDH2 and enter the membrane dimer formed by SDH3 and SDH4. Ref.3

Catalytic activity

Succinate + a quinone = fumarate + a quinol.

Cofactor

FAD.

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.

Miscellaneous

In vitro, can complement a SDH1 disruption and leads to less than 15% of wild-type SDH reductase activity probably due to its lower expression level (compared to SDH1).

Sequence similarities

Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion Potential
Chain26 – 634609Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial
PRO_0000010343

Regions

Nucleotide binding53 – 586FAD By similarity
Nucleotide binding76 – 9116FAD By similarity
Nucleotide binding443 – 4442FAD By similarity

Sites

Active site3251Proton acceptor By similarity
Binding site2601FAD By similarity
Binding site2811Substrate By similarity
Binding site2931Substrate By similarity
Binding site3921Substrate By similarity
Binding site4271FAD By similarity
Binding site4381Substrate By similarity

Amino acid modifications

Modified residue841Tele-8alpha-FAD histidine By similarity

Sequences

Sequence LengthMass (Da)Tools
P47052 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: F00CD157AB9BF9C5

FASTA63469,382
        10         20         30         40         50         60 
MLSLKKGITK SYILQRTFTS SSVVRQIGEV KSESKPPAKY HIIDHEYDCV VVGAGGAGLR 

        70         80         90        100        110        120 
AAFGLAEAGY KTACLSKLFP TRSHTVAAQG GINAALGNMH PDDWKSHMYD TVKGSDWLGD 

       130        140        150        160        170        180 
QDAIHYMTRE APKSVIELEH YGMPFSRTED GRIYQRAFGG QSKDFGKGGQ AYRTCAVADR 

       190        200        210        220        230        240 
TGHAMLHTLY GQALKNNTHF FIEYFAMDLL THNGEVVGVI AYNQEDGTIH RFRAHKTVIA 

       250        260        270        280        290        300 
TGGYGRAYFS CTSAHTCTGD GNAMVSRAGF PLEDLEFVQF HPSGIYGSGC LITEGARGEG 

       310        320        330        340        350        360 
GFLLNSEGER FMERYAPTAK DLASRDVVSR AITMEIRAGR GVGKNKDHIL LQLSHLPPEV 

       370        380        390        400        410        420 
LKERLPGISE TAAVFAGVDV TQEPIPVLPT VHYNMGGIPT KWTGEALTID EETGEDKVIP 

       430        440        450        460        470        480 
GLMACGEAAC VSVHGANRLG ANSLLDLVVF GRAVANTIAD TLQPGLPHKP LASNIGHESI 

       490        500        510        520        530        540 
ANLDKVRNAR GSLKTSQIRL NMQRTMQKDV SVFRTQDTLD EGVRNITEVD KTFEDVHVSD 

       550        560        570        580        590        600 
KSMIWNSDLV ETLELQNLLT CATQTAVSAS KRKESRGAHA REDYAKRDDV NWRKHTLSWQ 

       610        620        630 
KGTSTPVKIK YRNVIAHTLD ENECAPVPPA VRSY 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Suppression of sdh1 mutations by the SDH1b gene of Saccharomyces cerevisiae."
Colby G., Ishii Y., Tzagoloff A.
Yeast 14:1001-1006(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49320 Genomic DNA. Translation: CAA89336.1.
BK006943 Genomic DNA. Translation: DAA08755.1.
PIRS56817.
RefSeqNP_012490.1. NM_001181478.1.

3D structure databases

ProteinModelPortalP47052.
SMRP47052. Positions 39-634.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33713. 88 interactions.
DIPDIP-4262N.
IntActP47052. 1 interaction.
MINTMINT-501076.
STRING4932.YJL045W.

Proteomic databases

PaxDbP47052.
PeptideAtlasP47052.
PRIDEP47052.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL045W; YJL045W; YJL045W.
GeneID853405.
KEGGsce:YJL045W.

Organism-specific databases

CYGDYJL045w.
SGDS000003581. YJL045W.

Phylogenomic databases

eggNOGCOG1053.
GeneTreeENSGT00390000010046.
HOGENOMHOG000160475.
KOK00234.
OMAETIRWAE.
OrthoDBEOG7V76G3.

Enzyme and pathway databases

UniPathwayUPA00223; UER01006.

Gene expression databases

GenevestigatorP47052.

Family and domain databases

Gene3D1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProIPR003953. FAD_bind_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio973903.

Entry information

Entry nameSDHX_YEAST
AccessionPrimary (citable) accession number: P47052
Secondary accession number(s): D6VWD9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 14, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways