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P17412 (FRDA_WOLSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 flavoprotein subunit
EC=1.3.99.1
Gene names
Name:frdA
Ordered Locus Names:WS0831
OrganismWolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes) [Complete proteome] [HAMAP]
Taxonomic identifier273121 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Wolinella ›

Protein attributes

Sequence length656 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. Ref.2

Catalytic activity

Succinate + acceptor = fumarate + reduced acceptor.

Cofactor

Binds 1 FAD covalently per subunit.

Subunit structure

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

Sequence similarities

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

Ontologies

Keywords
   Biological processElectron transport
Respiratory chain
Transport
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentrespiratory chain

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionflavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

succinate dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 656656Fumarate reductase flavoprotein subunit
PRO_0000158667

Regions

Nucleotide binding9 – 2315FAD Potential

Sites

Active site2571 By similarity
Active site2731 By similarity

Amino acid modifications

Modified residue431Tele-8alpha-FAD histidine

Secondary structure

1 ............................................................................................................................. 656
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17412 [UniParc].

Last modified October 3, 2003. Version 3.
Checksum: BFEE6E8316F7F618

FASTA65672,719
        10         20         30         40         50         60 
MKVQYCDSLV IGGGLAGLRA AVATQQKGLS TIVLSLIPVK RSHSAAAQGG MQASLGNSKM 

        70         80         90        100        110        120 
SDGDNEDLHF MDTVKGSDWG CDQKVARMFV NTAPKAIREL AAWGVPWTRI HKGDRMAIIN 

       130        140        150        160        170        180 
AQKTTITEED FRHGLIHSRD FGGTKKWRTC YTADATGHTM LFAVANECLK LGVSIQDRKE 

       190        200        210        220        230        240 
AIALIHQDGK CYGAVVRDLV TGDIIAYVAK GTLIATGGYG RIYKNTTNAV VCEGTGTAIA 

       250        260        270        280        290        300 
LETGIAQLGN MEAVQFHPTP LFPSGILLTE GCRGDGGILR DVDGHRFMPD YEPEKKELAS 

       310        320        330        340        350        360 
RDVVSRRMIE HIRKGKGVQS PYGQHLWLDI SILGRKHIET NLRDVQEICE YFAGIDPAEK 

       370        380        390        400        410        420 
WAPVLPMQHY SMGGIRTDYR GEAKLKGLFS AGEAACWDMH GFNRLGGNSV SEAVVAGMIV 

       430        440        450        460        470        480 
GEYFAEHCAN TQVDLETKTL EKFVKGQEAY MKSLVESKGT EDVFKIKNRM KDVMDDNVGI 

       490        500        510        520        530        540 
FRDGPHLEKA VKELEELYKK SKNVGIKNKR LHANPELEEA YRVPMMLKVA LCVAKGALDR 

       550        560        570        580        590        600 
TESRGAHNRE DYPKRDDINW LNRTLASWPN PEQTLPTLEY EALDVNEMEI APGYRGYGAK 

       610        620        630        640        650 
GNYIENPLSV KRQEEIDKIQ SELEAAGKDR HAIQEALMPY ELPAKYKARN ERLGDK

« Hide

References

« Hide 'large scale' references
[1]"The fumarate reductase operon of Wolinella succinogenes. Sequence and expression of the frdA and frdB genes."
Lauterbach F., Koertner C., Albracht S.P., Unden G., Kroeger A.
Arch. Microbiol. 154:386-393(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon."
Simon J., Gross R., Ringel M., Schmidt E., Kroeger A.
Eur. J. Biochem. 251:418-426(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]Simon J.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 281-289; 490 AND 593.
[4]"Complete genome sequence and analysis of Wolinella succinogenes."
Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O., Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B., Meyer F., Lederer H., Schuster S.C.
Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W.
[5]"Cloning and expression of the genes of two fumarate reductase subunits from Wolinella succinogenes."
Lauterbach F., Kortner C., Tripier D., Unden G.
Eur. J. Biochem. 166:447-452(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
[6]"Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution."
Lancaster C.R.D., Kroeger A., Auer M., Michel H.
Nature 402:377-385(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SEQUENCE REVISION TO 281-289.
[7]"A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction."
Lancaster C.R.D., Gross R., Simon J.
Eur. J. Biochem. 268:1820-1827(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ000662 Genomic DNA. Translation: CAA04214.2.
BX571659 Genomic DNA. Translation: CAE09942.1.
M28294 Genomic DNA. Translation: AAA27586.1.
PIRB44954.
RefSeqNP_907042.1. NC_005090.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E7PX-ray3.10A/D/G/J1-656[»]
1QLBX-ray2.33A/D1-656[»]
2BS2X-ray1.78A/D1-656[»]
2BS3X-ray2.19A/D1-656[»]
2BS4X-ray2.76A/D1-656[»]
ProteinModelPortalP17412.
SMRP17412. Positions 1-655.
ModBaseSearch...

Protein-protein interaction databases

STRING273121.WS0831.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE09942; CAE09942; WS0831.
GeneID2555184.
KEGGwsu:WS0831.
PATRIC24038708. VBIWolSuc63014_0783.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1053.
HOGENOMHOG000160475.
KOK00244.
OMATNAVVCE.
ProtClustDBPRK08626.

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.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PANTHERPTHR11632:SF5. PTHR11632:SF5. 1 hit.
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF56425. SSF56425. 1 hit.
SSF46977. Succ_DH_flav_C. 1 hit.
TIGRFAMsTIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17412.

Entry information

Entry nameFRDA_WOLSU
AccessionPrimary (citable) accession number: P17412
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: October 3, 2003
Last modified: May 29, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents