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Protein

Sulfite reductase, dissimilatory-type subunit alpha

Gene

dsrA

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 bindingi176 – 1761Iron-sulfur (4Fe-4S) 1Combined sources2 Publications
Metal bindingi182 – 1821Iron-sulfur (4Fe-4S) 1Combined sources2 Publications
Metal bindingi220 – 2201Iron-sulfur (4Fe-4S) 1Combined sources2 Publications
Metal bindingi224 – 2241Iron (siroheme axial ligand)2 Publications
Metal bindingi224 – 2241Iron-sulfur (4Fe-4S) 1Combined sources2 Publications
Metal bindingi267 – 2671Iron-sulfur (4Fe-4S) 2Combined sources2 Publications
Metal bindingi286 – 2861Iron-sulfur (4Fe-4S) 2Combined sources2 Publications
Metal bindingi289 – 2891Iron-sulfur (4Fe-4S) 2Combined sources2 Publications
Metal bindingi292 – 2921Iron-sulfur (4Fe-4S) 2Combined sources2 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-434-MONOMER.
MetaCyc:MONOMER-12500.
BRENDAi1.8.99.1. 414.
1.8.99.3. 414.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite reductase, dissimilatory-type subunit alpha (EC:1.8.99.52 Publications)
Alternative name(s):
Dissimilatory sulfite reductase subunit alpha
Hydrogensulfite reductase subunit alpha
Gene namesi
Name:dsrA
Ordered Locus Names:AF_0423
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
Initiator methionineiRemoved1 Publication
Chaini2 – 418417Sulfite reductase, dissimilatory-type subunit alphaPRO_0000080025Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta subunits.2 Publications

Protein-protein interaction databases

STRINGi224325.AF0423.

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84Combined sources
Helixi9 – 113Combined sources
Beta strandi12 – 154Combined sources
Helixi18 – 3417Combined sources
Helixi44 – 5815Combined sources
Beta strandi75 – 795Combined sources
Turni84 – 885Combined sources
Helixi90 – 923Combined sources
Beta strandi96 – 1005Combined sources
Helixi104 – 1063Combined sources
Beta strandi107 – 1093Combined sources
Helixi110 – 12314Combined sources
Beta strandi126 – 1305Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi137 – 1426Combined sources
Helixi144 – 1463Combined sources
Helixi147 – 15610Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi167 – 1704Combined sources
Helixi178 – 1803Combined sources
Helixi189 – 19911Combined sources
Helixi201 – 2055Combined sources
Beta strandi209 – 2113Combined sources
Beta strandi215 – 2206Combined sources
Helixi227 – 2304Combined sources
Beta strandi232 – 24110Combined sources
Helixi247 – 2548Combined sources
Helixi259 – 2624Combined sources
Helixi264 – 2663Combined sources
Beta strandi272 – 2743Combined sources
Beta strandi279 – 2813Combined sources
Turni283 – 2853Combined sources
Helixi291 – 2955Combined sources
Turni297 – 2993Combined sources
Beta strandi304 – 3129Combined sources
Turni318 – 3203Combined sources
Beta strandi326 – 3327Combined sources
Helixi339 – 35517Combined sources
Helixi362 – 3698Combined sources
Helixi371 – 3777Combined sources
Helixi384 – 3863Combined sources
Beta strandi387 – 3893Combined sources
Helixi400 – 4023Combined sources
Helixi407 – 4159Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ59109.
SMRiQ59109. Positions 2-418.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59109.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini277 – 305294Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG02057. Archaea.
COG2221. LUCA.
KOiK11180.
OMAiMHCINVM.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR011806. DsrA.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
[Graphical view]
PfamiPF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 1 hit.
[Graphical view]
SUPFAMiSSF55124. SSF55124. 1 hit.
TIGRFAMsiTIGR02064. dsrA. 1 hit.
PROSITEiPS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q59109-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSETPLLDEL EKGPWPSFVK EIKKTAELME KAAAEGKDVK MPKGARGLLK
60 70 80 90 100
QLEISYKDKK THWKHGGIVS VVGYGGGVIG RYSDLGEQIP EVEHFHTMRI
110 120 130 140 150
NQPSGWFYST KALRGLCDVW EKWGSGLTNF HGSTGDIIFL GTRSEYLQPC
160 170 180 190 200
FEDLGNLEIP FDIGGSGSDL RTPSACMGPA LCEFACYDTL ELCYDLTMTY
210 220 230 240 250
QDELHRPMWP YKFKIKCAGC PNDCVASKAR SDFAIIGTWK DDIKVDQEAV
260 270 280 290 300
KEYASWMDIE NEVVKLCPTG AIKWDGKELT IDNRECVRCM HCINKMPKAL
310 320 330 340 350
KPGDERGATI LIGGKAPFVE GAVIGWVAVP FVEVEKPYDE IKEILEAIWD
360 370 380 390 400
WWDEEGKFRE RIGELIWRKG MREFLKVIGR EADVRMVKAP RNNPFMFFEK
410
DELKPSAYTE ELKKRGMW
Length:418
Mass (Da):47,525
Last modified:January 23, 2007 - v2
Checksum:iAC12A7BFDF27EEEF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95624 Genomic DNA. Translation: AAB17213.1.
AE000782 Genomic DNA. Translation: AAB90812.1.
PIRiG69302.
RefSeqiWP_010877930.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB90812; AAB90812; AF_0423.
GeneIDi24793961.
KEGGiafu:AF_0423.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95624 Genomic DNA. Translation: AAB17213.1.
AE000782 Genomic DNA. Translation: AAB90812.1.
PIRiG69302.
RefSeqiWP_010877930.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ59109.
SMRiQ59109. Positions 2-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF0423.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB90812; AAB90812; AF_0423.
GeneIDi24793961.
KEGGiafu:AF_0423.

Phylogenomic databases

eggNOGiarCOG02057. Archaea.
COG2221. LUCA.
KOiK11180.
OMAiMHCINVM.

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-434-MONOMER.
MetaCyc:MONOMER-12500.
BRENDAi1.8.99.1. 414.
1.8.99.3. 414.

Miscellaneous databases

EvolutionaryTraceiQ59109.

Family and domain databases

InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR011806. DsrA.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
[Graphical view]
PfamiPF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 1 hit.
[Graphical view]
SUPFAMiSSF55124. SSF55124. 1 hit.
TIGRFAMsiTIGR02064. dsrA. 1 hit.
PROSITEiPS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDSRA_ARCFU
AccessioniPrimary (citable) accession number: Q59109
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 109 of the entry and version 2 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.