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Protein

Sulfite reductase, dissimilatory-type subunit beta

Gene

dsrB

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration.1 Publication

Catalytic activityi

Hydrogen sulfide + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O = sulfite + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+.2 Publications
A [DsrC protein]-S-sulfanyl-L-cysteine + 3 acceptor + 3 H2O = sulfite + a [DsrC protein]-disulfide + 3 reduced acceptor + 2 H+.2 Publications

Cofactori

Protein has several cofactor binding sites:

Temperature dependencei

Highly thermostable. Inactive towards methylviologen below 55 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi140 – 1401Iron-sulfur (4Fe-4S) 1Combined sources2 Publications
Metal bindingi177 – 1771Iron-sulfur (4Fe-4S) 1Combined sources2 Publications
Metal bindingi178 – 1781Iron-sulfur (4Fe-4S) 1Combined sources2 Publications
Metal bindingi182 – 1821Iron (siroheme axial ligand)2 Publications
Metal bindingi182 – 1821Iron-sulfur (4Fe-4S) 1Combined sources2 Publications
Metal bindingi220 – 2201Iron-sulfur (4Fe-4S) 2Combined sources2 Publications
Metal bindingi241 – 2411Iron-sulfur (4Fe-4S) 2Combined sources2 Publications
Metal bindingi244 – 2441Iron-sulfur (4Fe-4S) 2Combined sources2 Publications
Metal bindingi247 – 2471Iron-sulfur (4Fe-4S) 2Combined sources2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

4Fe-4S, Heme, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-435-MONOMER.
MetaCyc:MONOMER-12501.
BRENDAi1.8.99.3. 414.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite reductase, dissimilatory-type subunit beta (EC:1.8.99.52 Publications)
Alternative name(s):
Hydrogensulfite reductase subunit beta
Gene namesi
Name:dsrB
Ordered Locus Names:AF_0424
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

Subcellular locationi

  • Membrane

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Sulfite reductase, dissimilatory-type subunit betaPRO_0000080027Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta subunits.2 Publications

Protein-protein interaction databases

STRINGi224325.AF0424.

Structurei

Secondary structure

1
366
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 184Combined sources
Helixi21 – 266Combined sources
Beta strandi30 – 378Combined sources
Beta strandi40 – 456Combined sources
Beta strandi50 – 567Combined sources
Beta strandi60 – 634Combined sources
Helixi64 – 7714Combined sources
Beta strandi81 – 844Combined sources
Beta strandi90 – 956Combined sources
Helixi97 – 993Combined sources
Helixi100 – 11112Combined sources
Turni121 – 1244Combined sources
Helixi136 – 1394Combined sources
Helixi148 – 15710Combined sources
Helixi159 – 1635Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi173 – 1786Combined sources
Beta strandi182 – 1843Combined sources
Helixi185 – 1873Combined sources
Beta strandi188 – 1958Combined sources
Helixi204 – 2107Combined sources
Helixi213 – 2186Combined sources
Beta strandi225 – 2284Combined sources
Turni229 – 2324Combined sources
Beta strandi233 – 2364Combined sources
Helixi238 – 2403Combined sources
Helixi246 – 2505Combined sources
Turni259 – 2613Combined sources
Beta strandi263 – 2686Combined sources
Beta strandi275 – 2773Combined sources
Beta strandi283 – 2908Combined sources
Turni293 – 2953Combined sources
Helixi297 – 31317Combined sources
Helixi320 – 3278Combined sources
Helixi329 – 3368Combined sources
Helixi342 – 3443Combined sources
Beta strandi350 – 3523Combined sources
Helixi353 – 3575Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MM5X-ray1.80B/E1-366[»]
3MM6X-ray1.90B/E1-366[»]
3MM7X-ray1.90B/E1-366[»]
3MM8X-ray2.28B/E1-366[»]
3MM9X-ray2.10B/E1-366[»]
3MMAX-ray2.30B/E1-366[»]
3MMBX-ray2.30B/E1-366[»]
3MMCX-ray2.04B/E1-366[»]
ProteinModelPortaliQ59110.
SMRiQ59110. Positions 4-366.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59110.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini232 – 262314Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 4Fe-4S ferredoxin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiarCOG02059. Archaea.
COG2221. LUCA.
KOiK11181.
OMAiWLHCDIP.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR011808. DsrB.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
[Graphical view]
PfamiPF00037. Fer4. 1 hit.
PF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 1 hit.
[Graphical view]
SUPFAMiSSF55124. SSF55124. 1 hit.
TIGRFAMsiTIGR02066. dsrB. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59110-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVEGVKTDF GPPYFRDLLH PVIAKNYGKW KYHEVVKPGV IKRVAESGDV
60 70 80 90 100
IYVVRFGTPR LLSIYTVREL CDIADKYSDG YLRWTSRNNV EFFVTDESKI
110 120 130 140 150
DDLINEVQER VGFPCGGTWD AVKGEYGLSN IVHTQGWIHC HTPAIDASGI
160 170 180 190 200
VKAVMDELYE YFTDHKLPAM CRISLACCAN MCGAVHASDI AIVGIHRTPP
210 220 230 240 250
IPNDEAIRKT CEIPSTVAAC PTGALKPDMK NKTIKVDVEK CMYCGNCYTM
260 270 280 290 300
CPGMPLFDPE NDGAAIMVGG KLSEARRMPE LSKVVVPWVP NEPPRWPTLV
310 320 330 340 350
KYVKQILEAW AANANKHERL IEWVDRIGWE RFFELTGLEF TQHLIDDYRI
360
TPYFYSEFRA STQFKW
Length:366
Mass (Da):41,570
Last modified:November 1, 1996 - v1
Checksum:iBA8E4C59216459DA
GO

Sequence cautioni

The sequence AAB90811.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95624 Genomic DNA. Translation: AAB17214.1.
AE000782 Genomic DNA. Translation: AAB90811.1. Different initiation.
PIRiH69302.
RefSeqiWP_048064231.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB90811; AAB90811; AF_0424.
GeneIDi24793962.
KEGGiafu:AF_0424.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95624 Genomic DNA. Translation: AAB17214.1.
AE000782 Genomic DNA. Translation: AAB90811.1. Different initiation.
PIRiH69302.
RefSeqiWP_048064231.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MM5X-ray1.80B/E1-366[»]
3MM6X-ray1.90B/E1-366[»]
3MM7X-ray1.90B/E1-366[»]
3MM8X-ray2.28B/E1-366[»]
3MM9X-ray2.10B/E1-366[»]
3MMAX-ray2.30B/E1-366[»]
3MMBX-ray2.30B/E1-366[»]
3MMCX-ray2.04B/E1-366[»]
ProteinModelPortaliQ59110.
SMRiQ59110. Positions 4-366.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF0424.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB90811; AAB90811; AF_0424.
GeneIDi24793962.
KEGGiafu:AF_0424.

Phylogenomic databases

eggNOGiarCOG02059. Archaea.
COG2221. LUCA.
KOiK11181.
OMAiWLHCDIP.

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-435-MONOMER.
MetaCyc:MONOMER-12501.
BRENDAi1.8.99.3. 414.

Miscellaneous databases

EvolutionaryTraceiQ59110.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR011808. DsrB.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
[Graphical view]
PfamiPF00037. Fer4. 1 hit.
PF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 1 hit.
[Graphical view]
SUPFAMiSSF55124. SSF55124. 1 hit.
TIGRFAMsiTIGR02066. dsrB. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 332-359, FUNCTION, CATALYTIC ACTIVITY.
    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.
    , 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.
  3. "Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus."
    Schiffer A., Parey K., Warkentin E., Diederichs K., Huber H., Stetter K.O., Kroneck P.M.H., Ermler U.
    J. Mol. Biol. 379:1063-1074(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S) AND SIROHEME, SUBUNIT, COFACTOR, REACTION MECHANISM.
  4. "Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus."
    Parey K., Warkentin E., Kroneck P.M., Ermler U.
    Biochemistry 49:8912-8921(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH DSRB; IRON-SULFUR (4FE-4S); SIROHEME AND HYDROGENSULFITE, COFACTOR, SUBUNIT, CATALYTIC ACTIVITY, REACTION MECHANISM.

Entry informationi

Entry nameiDSRB_ARCFU
AccessioniPrimary (citable) accession number: Q59110
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: December 9, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.