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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)DescriptionActionsGraphical viewLength
Metal bindingi176Iron-sulfur (4Fe-4S) 1Combined sources2 Publications1
Metal bindingi182Iron-sulfur (4Fe-4S) 1Combined sources2 Publications1
Metal bindingi220Iron-sulfur (4Fe-4S) 1Combined sources2 Publications1
Metal bindingi224Iron (siroheme axial ligand)2 Publications1
Metal bindingi224Iron-sulfur (4Fe-4S) 1Combined sources2 Publications1
Metal bindingi267Iron-sulfur (4Fe-4S) 2Combined sources2 Publications1
Metal bindingi286Iron-sulfur (4Fe-4S) 2Combined sources2 Publications1
Metal bindingi289Iron-sulfur (4Fe-4S) 2Combined sources2 Publications1
Metal bindingi292Iron-sulfur (4Fe-4S) 2Combined sources2 Publications1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc: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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000800252 – 418Sulfite reductase, dissimilatory-type subunit alphaAdd BLAST417

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta subunits.2 Publications

Protein-protein interaction databases

STRINGi224325.AF0423.

Structurei

Secondary structure

1418
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 8Combined sources4
Helixi9 – 11Combined sources3
Beta strandi12 – 15Combined sources4
Helixi18 – 34Combined sources17
Helixi44 – 58Combined sources15
Beta strandi75 – 79Combined sources5
Turni84 – 88Combined sources5
Helixi90 – 92Combined sources3
Beta strandi96 – 100Combined sources5
Helixi104 – 106Combined sources3
Beta strandi107 – 109Combined sources3
Helixi110 – 123Combined sources14
Beta strandi126 – 130Combined sources5
Beta strandi133 – 135Combined sources3
Beta strandi137 – 142Combined sources6
Helixi144 – 146Combined sources3
Helixi147 – 156Combined sources10
Beta strandi157 – 159Combined sources3
Beta strandi167 – 170Combined sources4
Helixi178 – 180Combined sources3
Helixi189 – 199Combined sources11
Helixi201 – 205Combined sources5
Beta strandi209 – 211Combined sources3
Beta strandi215 – 220Combined sources6
Helixi227 – 230Combined sources4
Beta strandi232 – 241Combined sources10
Helixi247 – 254Combined sources8
Helixi259 – 262Combined sources4
Helixi264 – 266Combined sources3
Beta strandi272 – 274Combined sources3
Beta strandi279 – 281Combined sources3
Turni283 – 285Combined sources3
Helixi291 – 295Combined sources5
Turni297 – 299Combined sources3
Beta strandi304 – 312Combined sources9
Turni318 – 320Combined sources3
Beta strandi326 – 332Combined sources7
Helixi339 – 355Combined sources17
Helixi362 – 369Combined sources8
Helixi371 – 377Combined sources7
Helixi384 – 386Combined sources3
Beta strandi387 – 389Combined sources3
Helixi400 – 402Combined sources3
Helixi407 – 415Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59109.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini277 – 3054Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd BLAST29

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
PDB 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.
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

BioCyciMetaCyc: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: November 2, 2016
This is version 111 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.