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

Q7ZVF3 (SDHA_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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] flavoprotein subunit, mitochondrial

EC=1.3.5.1
Alternative name(s):
Flavoprotein subunit of complex II
Short name=Fp
Gene names
Name:sdha
ORF Names:si:dkeyp-84f11.2
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length661 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Flavoprotein (FP) 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 + a quinone = fumarate + a quinol.

Cofactor

FAD 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: the flavoprotein (FP) sdha, iron-sulfur protein (IP) sdhb, and a cytochrome b560 composed of sdhc and sdhd. Interacts with sdhaf2/sdh5; interaction is required for FAD attachment By similarity.

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity.

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 – 4040Mitochondrion By similarity
Chain41 – 661621Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
PRO_0000344985

Regions

Nucleotide binding65 – 706FAD By similarity
Nucleotide binding88 – 10316FAD By similarity
Nucleotide binding453 – 4542FAD By similarity

Sites

Active site3371Proton acceptor By similarity
Binding site2721FAD By similarity
Binding site2931Substrate By similarity
Binding site3051Substrate By similarity
Binding site4041Substrate By similarity
Binding site4371FAD By similarity
Binding site4481Substrate By similarity

Amino acid modifications

Modified residue961Tele-8alpha-FAD histidine By similarity

Experimental info

Sequence conflict181C → S in AAH45885. Ref.2
Sequence conflict5451D → N in AAH45885. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q7ZVF3 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: 636BF993BE55D19B

FASTA66172,078
        10         20         30         40         50         60 
MAAVCAASRV LGTKILSCKS LPAVCQANRQ LHFSIYGKRG DAKISDGVSN QYPVVDHEFD 

        70         80         90        100        110        120 
AVVVGAGGAG LRAAFGLSEA GFNTACVTKL FPTRSHTVAA QGGINAALGN MEQDDWRWHF 

       130        140        150        160        170        180 
YDTVKGSDWL GDQDAIHYMT EQAPAAVVEL ENFGMPFSRT DDGKIYQRAF GGQSLKFGKG 

       190        200        210        220        230        240 
GQAHRCCCVA DRTGHSLLHT LYGRSLRYDT SYFVEYFALD LLMEDGECKG VIALCMEDGS 

       250        260        270        280        290        300 
IHRFRAKNTV IATGGYGRTF FSCTSAHTST GDGNAMVTRA GLPCQDLEFV QFHPTGIYGA 

       310        320        330        340        350        360 
GCLITEGCRG EGGILINSEG ERFMERYAPN AKDLASRDVV SRSMTIEIRE GRGVGPDKDH 

       370        380        390        400        410        420 
VHLQLHHLPP QQLAARLPGI SETAMIFAGV DVTKEPIPVL PTVHYNMGGI PTNYKGQVIT 

       430        440        450        460        470        480 
YKDGQDHVVP GLYACGEAGC ASVHGANRLG ANSLLDLVVF GRACALTIAE IDTPGEKLSP 

       490        500        510        520        530        540 
LKPNAGEASV ANLDKMRYAN GSTRTSEIRL NMQKTMQSHA AVFRTGDVLK EGCVKMESVY 

       550        560        570        580        590        600 
KSMDDIKTFD RGIVWNTDLV ETLELQNLML NAVQTIVSAE ARKESRGAHA REDFKDRVDE 

       610        620        630        640        650        660 
YDYSKPLQGQ VKKPFEQHWR KHTLSYVDPE TGKVTLEYRP VIDSSLDAED CAAIPPAIRS 


Y 

« Hide

References

[1]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: AB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX890617 Genomic DNA. Translation: CAK11468.1.
BC045885 mRNA. Translation: AAH45885.1.
RefSeqNP_957204.1. NM_200910.1.
UniGeneDr.105233.

3D structure databases

ProteinModelPortalQ7ZVF3.
SMRQ7ZVF3. Positions 51-661.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ7ZVF3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000015559; ENSDARP00000018027; ENSDARG00000016721.
GeneID393884.
KEGGdre:393884.

Organism-specific databases

CTD6389.
ZFINZDB-GENE-040426-874. sdha.

Phylogenomic databases

eggNOGCOG1053.
GeneTreeENSGT00390000010046.
HOGENOMHOG000160475.
HOVERGENHBG001461.
KOK00234.
OMAINVFGKR.
OrthoDBEOG7MH0XJ.
TreeFamTF300763.

Enzyme and pathway databases

UniPathwayUPA00223; UER01006.

Gene expression databases

BgeeQ7ZVF3.

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

NextBio20814864.
PROQ7ZVF3.

Entry information

Entry nameSDHA_DANRE
AccessionPrimary (citable) accession number: Q7ZVF3
Secondary accession number(s): Q1LV99
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: April 16, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways