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P0AC50 (FRDB_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Fumarate reductase iron-sulfur subunit

EC=1.3.5.1
Gene names
Name:frdB
Ordered Locus Names:SF4311, S4576
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth By similarity.

Catalytic activity

Succinate + a quinone = fumarate + a quinol.

Cofactor

Binds 1 2Fe-2S cluster By similarity.

Binds 1 3Fe-4S cluster By similarity.

Binds 1 4Fe-4S cluster By similarity.

Subunit structure

Fumarate dehydrogenase forms part of an enzyme complex containing four subunits: a flavoprotein, an iron-sulfur, and two hydrophobic anchor proteins 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

Initiator methionine11Removed By similarity
Chain2 – 244243Fumarate reductase iron-sulfur subunit
PRO_0000158701

Regions

Domain16 – 97822Fe-2S ferredoxin-type
Domain140 – 169304Fe-4S ferredoxin-type

Sites

Metal binding581Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding631Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding661Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding781Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1491Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1521Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1551Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1591Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2051Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2111Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2151Iron-sulfur 2 (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AC50 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AC1D7A73244D7AC0

FASTA24427,123
        10         20         30         40         50         60 
MAEMKNLKIE VVRYNPEVDT APHSAFYEVP YDATTSLLDA LGYIKDNLAP DLSYRWSCRM 

        70         80         90        100        110        120 
AICGSCGMMV NNVPKLACKT FLRDYTDGMK VEALANFPIE RDLVVDMTHF IESLEAIKPY 

       130        140        150        160        170        180 
IIGNSRTADQ GTNIQTPAQM AKYHQFSGCI NCGLCYAACP QFGLNPEFIG PAAITLAHRY 

       190        200        210        220        230        240 
NEDSRDHGKK ERMAQLNSQN GVWSCTFVGY CSEVCPKHVD PAAAIQQGKV ESSKDFLIAT 


LKPR 

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN45729.2.
AE014073 Genomic DNA. Translation: AAP19513.1.
RefSeqNP_710022.2. NC_004337.2.
NP_839701.1. NC_004741.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF4311.

Proteomic databases

PaxDbP0AC50.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN45729; AAN45729; SF4311.
AAP19513; AAP19513; S4576.
GeneID1026842.
1080783.
KEGGsfl:SF4311.
sfx:S4576.
PATRIC18711184. VBIShiFle31049_4994.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0479.
HOGENOMHOG000160590.
KOK00245.
OrthoDBEOG6CK7MG.

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.
PF13183. Fer4_8. 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 nameFRDB_SHIFL
AccessionPrimary (citable) accession number: P0AC50
Secondary accession number(s): P00364
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 62 of the entry and version 2 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