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

Q92J97 (SDHA_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 flavoprotein subunit

EC=1.3.5.1
Gene names
Name:sdhA
Ordered Locus Names:RC0170
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length596 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Succinate + a quinone = fumarate + a quinol.

Cofactor

FAD.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (bacterial route): step 1/1.

Subunit structure

Part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, cytochrome b-556, and a hydrophobic anchor protein.

Subcellular location

Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.

Sequence similarities

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 596596Succinate dehydrogenase flavoprotein subunit
PRO_0000158656

Regions

Nucleotide binding18 – 236FAD By similarity
Nucleotide binding41 – 5616FAD By similarity
Nucleotide binding407 – 4082FAD By similarity

Sites

Active site2901Proton acceptor By similarity
Binding site2251FAD By similarity
Binding site2461Substrate By similarity
Binding site2581Substrate By similarity
Binding site3571Substrate By similarity
Binding site3911FAD By similarity
Binding site4021Substrate By similarity

Amino acid modifications

Modified residue491Tele-8alpha-FAD histidine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92J97 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F313CE9506A7DA10

FASTA59665,291
        10         20         30         40         50         60 
MTKAYNIIHH KFDVVVVGAG GAGLRSAFGM AKEGLNTACI TKLFPTRSHT VAAQGGISAA 

        70         80         90        100        110        120 
LGNMGEDDWR WHMYDTVKGS DWLGDQDAIE YMCKNAPDAI LELEHYGVPF SRTEEGKIYQ 

       130        140        150        160        170        180 
RPFGGMTTEY GKGKAAQRTC AAADRTGHAI LHTLYQQSLK HKVQFFVEYF AIDLLMEDGE 

       190        200        210        220        230        240 
CRGVVAWNLD DGSLHCFRAH NVVLATGGYG RAYFSATSAH TCTGDGGGMA IRAGLPLQDM 

       250        260        270        280        290        300 
EFVQFHPTGI YSAGCLITEG ARGEGGYLVN ANGERFMERY APAAKDLASR DVVSRAMTIE 

       310        320        330        340        350        360 
IREGRGVGEH KDHVFLHLNH LSPEILHSRL PGISETAKIF AGVDVTKEPI PVLPTVHYNM 

       370        380        390        400        410        420 
GGIPTNYHGQ VIIKDGKNHN SVVKGLMAIG EAACVSVHGA NRLGSNSLLD LVVFGRSSAL 

       430        440        450        460        470        480 
KAAELIKPAS PHRSIKEESL EKIINRFDKV RHANGNILVA ELRLKMQRTM QSHASVFRTQ 

       490        500        510        520        530        540 
EVLDEGAGMI SEIRSGYKDI KINDKSLIWN SDLVEALELD NLLDQALVTV YSAAARKESR 

       550        560        570        580        590 
GAHAREDYPD RNDEDWMKHT LSSIDEAGKV VLDYKPVTLT TLTDEVTAVP PVKRVY 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL02708.1.
PIRB97721.
RefSeqNP_359807.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92J97.
SMRQ92J97. Positions 5-596.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC0170.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL02708; AAL02708; RC0170.
GeneID928018.
KEGGrco:RC0170.
PATRIC17887475. VBIRicCon45613_0199.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1053.
HOGENOMHOG000160475.
KOK00239.
OMASYRPVHV.
OrthoDBEOG6M3PC4.

Enzyme and pathway databases

UniPathwayUPA00223; UER01005.

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...

Entry information

Entry nameSDHA_RICCN
AccessionPrimary (citable) accession number: Q92J97
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: December 1, 2001
Last modified: May 14, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Rickettsia conorii

(strain Malish 7): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways