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Protein

Sulfite reductase, dissimilatory-type subunit alpha

Gene

dsvA

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Part of the complex that catalyzes the reduction of sulfite to sulfide. The alpha and beta subunits may have arisen by gene duplication. They both bind 2 iron-sulfur clusters, but the alpha subunit seems to be catalytically inactive, due to substitutions along the putative substrate access channel, and because it binds sirohydrochlorin (the dematallated form of siroheme) instead of siroheme.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi177 – 1771Iron-sulfur (4Fe-4S) 1Combined sources1 Publication
Metal bindingi183 – 1831Iron-sulfur (4Fe-4S) 1Combined sources1 Publication
Metal bindingi221 – 2211Iron-sulfur (4Fe-4S) 1Combined sources1 Publication
Metal bindingi225 – 2251Iron-sulfur (4Fe-4S) 1Combined sources1 Publication
Metal bindingi284 – 2841Iron-sulfur (4Fe-4S) 2Combined sources1 Publication
Metal bindingi303 – 3031Iron-sulfur (4Fe-4S) 2Combined sources1 Publication
Metal bindingi306 – 3061Iron-sulfur (4Fe-4S) 2Combined sources1 Publication
Metal bindingi309 – 3091Iron-sulfur (4Fe-4S) 2Combined sources1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciDVUL882:GJIL-422-MONOMER.
MetaCyc:MONOMER-12511.
BRENDAi1.8.99.3. 1914.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfite reductase, dissimilatory-type subunit alpha
Alternative name(s):
Desulfoviridin subunit alpha
Dissimilatory sulfite reductase subunit alpha1 Publication
Short name:
dSiR alpha1 Publication
Hydrogensulfite reductase subunit alpha
Gene namesi
Name:dsvA
Synonyms:dsrA1 Publication
Ordered Locus Names:DVU_0402
OrganismiDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Taxonomic identifieri882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
Proteomesi
  • UP000002194 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 437436Sulfite reductase, dissimilatory-type subunit alphaPRO_0000080030Add
BLAST

Proteomic databases

PaxDbiP45574.

Interactioni

Subunit structurei

Heterohexamer of two alpha, two beta and two gamma subunits.2 Publications

Protein-protein interaction databases

IntActiP45574. 4 interactions.
STRINGi882.DVU0402.

Structurei

Secondary structure

1
437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 135Combined sources
Beta strandi14 – 174Combined sources
Helixi20 – 3314Combined sources
Helixi46 – 6015Combined sources
Beta strandi79 – 813Combined sources
Beta strandi84 – 874Combined sources
Turni88 – 903Combined sources
Helixi92 – 943Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi109 – 1113Combined sources
Helixi112 – 12514Combined sources
Beta strandi128 – 1325Combined sources
Beta strandi139 – 1424Combined sources
Helixi146 – 1483Combined sources
Helixi149 – 15810Combined sources
Beta strandi168 – 1714Combined sources
Helixi179 – 1813Combined sources
Helixi190 – 20011Combined sources
Helixi202 – 2065Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi216 – 2216Combined sources
Helixi228 – 2314Combined sources
Beta strandi233 – 24210Combined sources
Helixi248 – 2558Combined sources
Helixi261 – 2644Combined sources
Turni265 – 2684Combined sources
Helixi276 – 2794Combined sources
Helixi281 – 2833Combined sources
Beta strandi289 – 2913Combined sources
Beta strandi296 – 2983Combined sources
Helixi300 – 3023Combined sources
Helixi308 – 3125Combined sources
Turni314 – 3163Combined sources
Beta strandi321 – 3299Combined sources
Turni335 – 3373Combined sources
Beta strandi343 – 3497Combined sources
Helixi356 – 37217Combined sources
Helixi379 – 3868Combined sources
Helixi388 – 3947Combined sources
Helixi401 – 4033Combined sources
Beta strandi404 – 4063Combined sources
Helixi417 – 4193Combined sources
Helixi428 – 4347Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4JX-ray2.10A/D1-437[»]
ProteinModelPortaliP45574.
SMRiP45574. Positions 5-436.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45574.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini294 – 322294Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CY1. Bacteria.
COG2221. LUCA.
KOiK11180.
OMAiMHCINVM.
OrthoDBiPOG091H10BN.

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.

P45574-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKHATPKLD QLESGPWPSF VSDIKQEAAY RAANPKGLDY QVPVDCPEDL
60 70 80 90 100
LGVLELSYDE GETHWKHGGI VGVFGYGGGV IGRYCDQPEK FPGVAHFHTV
110 120 130 140 150
RVAQPSGKYY SADYLRQLCD IWDLRGSGLT NMHGSTGDIV LLGTQTPQLE
160 170 180 190 200
EIFFELTHNL NTDLGGSGSN LRTPESCLGK SRCEFACYDS QAACYELTME
210 220 230 240 250
YQDELHRPAF PYKFKFKFDA CPNGCVASIA RSDFSVIGTW KDDIKIDAEA
260 270 280 290 300
VKAYVAGEFK PNAGAHSGRD WGKFDIEAEV VNRCPSKCMK WDGSKLSIDN
310 320 330 340 350
KECVRCMHCI NTMPRALHIG DERGASILCG AKAPILDGAQ MGSLLVPFVA
360 370 380 390 400
AEEPFDEIKE VVEKIWDWWM EEGKNRERLG ETMKRLSFQK LLEVTEIAPV
410 420 430
PQHVKEPRTN PYIFFKEEEV PGGWDRDITE YRKRHLR
Length:437
Mass (Da):49,091
Last modified:January 23, 2007 - v3
Checksum:i4AED624D4B13A21F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221S → V AA sequence (PubMed:1555572).Curated
Sequence conflicti26 – 261Q → K AA sequence (PubMed:1555572).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16723 Genomic DNA. Translation: AAA70107.1.
AE017285 Genomic DNA. Translation: AAS94885.1.
PIRiS21197.
RefSeqiWP_010937709.1. NC_002937.3.
YP_009626.1. NC_002937.3.

Genome annotation databases

EnsemblBacteriaiAAS94885; AAS94885; DVU_0402.
GeneIDi2796152.
KEGGidvu:DVU0402.
PATRICi32060772. VBIDesVul119526_0379.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16723 Genomic DNA. Translation: AAA70107.1.
AE017285 Genomic DNA. Translation: AAS94885.1.
PIRiS21197.
RefSeqiWP_010937709.1. NC_002937.3.
YP_009626.1. NC_002937.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4JX-ray2.10A/D1-437[»]
ProteinModelPortaliP45574.
SMRiP45574. Positions 5-436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP45574. 4 interactions.
STRINGi882.DVU0402.

Proteomic databases

PaxDbiP45574.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS94885; AAS94885; DVU_0402.
GeneIDi2796152.
KEGGidvu:DVU0402.
PATRICi32060772. VBIDesVul119526_0379.

Phylogenomic databases

eggNOGiENOG4105CY1. Bacteria.
COG2221. LUCA.
KOiK11180.
OMAiMHCINVM.
OrthoDBiPOG091H10BN.

Enzyme and pathway databases

BioCyciDVUL882:GJIL-422-MONOMER.
MetaCyc:MONOMER-12511.
BRENDAi1.8.99.3. 1914.

Miscellaneous databases

EvolutionaryTraceiP45574.

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 nameiDSVA_DESVH
AccessioniPrimary (citable) accession number: P45574
Secondary accession number(s): Q46581
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 101 of the entry and version 3 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.