Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q59109 (DSRA_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfite reductase, dissimilatory-type subunit alpha
EC=1.8.99.3
Alternative name(s):
Hydrogensulfite reductase subunit alpha
Gene names
Name:dsrA
Ordered Locus Names:AF_0423
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [Reference proteome] [HAMAP]
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus ›

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration.

Catalytic activity

(O3S.S.SO3)2- + acceptor + 2 H2O + OH- = 3 HSO3- + reduced acceptor.

Cofactor

Binds 1 4Fe-4S cluster per subunit.

Binds 2 sirohemes per subunit.

Subunit structure

Heterotetramer of two alpha and two beta subunits.

Subcellular location

Membrane. Note: Although the protein complex is found in the soluble fraction it may be membrane-associated in vivo.

Sequence similarities

Contains 1 4Fe-4S ferredoxin-type domain.

Biophysicochemical properties

Temperature dependence:

Highly thermostable. Inactive towards methylviologen below 55 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 418417Sulfite reductase, dissimilatory-type subunit alpha
PRO_0000080025

Regions

Domain277 – 305294Fe-4S ferredoxin-type

Sites

Metal binding1761Iron (heme axial ligand) Potential
Metal binding1821Iron (heme axial ligand) Potential
Metal binding2201Iron (heme axial ligand) Potential
Metal binding2241Iron (heme axial ligand) Potential
Metal binding2671Iron-sulfur (4Fe-4S) Potential
Metal binding2861Iron-sulfur (4Fe-4S) Potential
Metal binding2891Iron-sulfur (4Fe-4S) Potential
Metal binding2921Iron-sulfur (4Fe-4S) Potential

Secondary structure

1 .................................................................................. 418
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q59109 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AC12A7BFDF27EEEF

FASTA41847,525
        10         20         30         40         50         60 
MSETPLLDEL EKGPWPSFVK EIKKTAELME KAAAEGKDVK MPKGARGLLK QLEISYKDKK 

        70         80         90        100        110        120 
THWKHGGIVS VVGYGGGVIG RYSDLGEQIP EVEHFHTMRI NQPSGWFYST KALRGLCDVW 

       130        140        150        160        170        180 
EKWGSGLTNF HGSTGDIIFL GTRSEYLQPC FEDLGNLEIP FDIGGSGSDL RTPSACMGPA 

       190        200        210        220        230        240 
LCEFACYDTL ELCYDLTMTY QDELHRPMWP YKFKIKCAGC PNDCVASKAR SDFAIIGTWK 

       250        260        270        280        290        300 
DDIKVDQEAV KEYASWMDIE NEVVKLCPTG AIKWDGKELT IDNRECVRCM HCINKMPKAL 

       310        320        330        340        350        360 
KPGDERGATI LIGGKAPFVE GAVIGWVAVP FVEVEKPYDE IKEILEAIWD WWDEEGKFRE 

       370        380        390        400        410 
RIGELIWRKG MREFLKVIGR EADVRMVKAP RNNPFMFFEK DELKPSAYTE ELKKRGMW

« Hide

References

« Hide 'large scale' references
[1]"Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes."
Dahl C., Kredich N.M., Deutzmann R., Trueper H.G.
J. Gen. Microbiol. 139:1817-1828(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-37; 65-71; 82-99; 124-141; 344-355; 362-368 AND 392-413.
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. expand/collapse author list , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M95624 Genomic DNA. Translation: AAB17213.1.
AE000782 Genomic DNA. Translation: AAB90812.1.
PIRG69302.
RefSeqNP_069259.1. NC_000917.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MM5X-ray1.80A/D1-418[»]
3MM6X-ray1.90A/D1-418[»]
3MM7X-ray1.90A/D1-418[»]
3MM8X-ray2.28A/D1-418[»]
3MM9X-ray2.10A/D1-418[»]
3MMAX-ray2.30A/D1-418[»]
3MMBX-ray2.30A/D1-418[»]
3MMCX-ray2.04A/D1-418[»]
ProteinModelPortalQ59109.
SMRQ59109. Positions 2-418.
ModBaseSearch...

Protein-protein interaction databases

STRING224325.AF0423.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB90812; AAB90812; AF_0423.
GeneID1483639.
KEGGafu:AF0423.

Phylogenomic databases

eggNOGCOG2221.
KOK11180.
OMADIMLQGI.
ProtClustDBCLSK862600.

Enzyme and pathway databases

BioCycAFUL224325:GJBC-434-MONOMER.
MetaCyc:MONOMER-12500.

Family and domain databases

InterProIPR017896. 4Fe4S_Fe-S-bd.
IPR011806. DsrA.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
[Graphical view]
PfamPF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 1 hit.
[Graphical view]
TIGRFAMsTIGR02064. dsrA. 1 hit.
PROSITEPS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ59109.

Entry information

Entry nameDSRA_ARCFU
AccessionPrimary (citable) accession number: Q59109
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 95 of the entry and version 2 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