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Protein

Sulfite reductase, dissimilatory-type subunit alpha

Gene

dsvA

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / 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)DescriptionActionsGraphical viewLength
Metal bindingi177Iron-sulfur (4Fe-4S) 1Combined sources1 Publication1
Metal bindingi183Iron-sulfur (4Fe-4S) 1Combined sources1 Publication1
Metal bindingi221Iron-sulfur (4Fe-4S) 1Combined sources1 Publication1
Metal bindingi225Iron-sulfur (4Fe-4S) 1Combined sources1 Publication1
Metal bindingi284Iron-sulfur (4Fe-4S) 2Combined sources1 Publication1
Metal bindingi303Iron-sulfur (4Fe-4S) 2Combined sources1 Publication1
Metal bindingi306Iron-sulfur (4Fe-4S) 2Combined sources1 Publication1
Metal bindingi309Iron-sulfur (4Fe-4S) 2Combined sources1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc: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 / DSM 644 / NCIMB 8303)
Taxonomic identifieri882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
Proteomesi
  • UP000002194 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000800302 – 437Sulfite reductase, dissimilatory-type subunit alphaAdd BLAST436

Proteomic databases

PaxDbiP45574.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP45574. 4 interactors.
STRINGi882.DVU0402.

Structurei

Secondary structure

1437
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 13Combined sources5
Beta strandi14 – 17Combined sources4
Helixi20 – 33Combined sources14
Helixi46 – 60Combined sources15
Beta strandi79 – 81Combined sources3
Beta strandi84 – 87Combined sources4
Turni88 – 90Combined sources3
Helixi92 – 94Combined sources3
Beta strandi99 – 102Combined sources4
Beta strandi109 – 111Combined sources3
Helixi112 – 125Combined sources14
Beta strandi128 – 132Combined sources5
Beta strandi139 – 142Combined sources4
Helixi146 – 148Combined sources3
Helixi149 – 158Combined sources10
Beta strandi168 – 171Combined sources4
Helixi179 – 181Combined sources3
Helixi190 – 200Combined sources11
Helixi202 – 206Combined sources5
Beta strandi210 – 212Combined sources3
Beta strandi216 – 221Combined sources6
Helixi228 – 231Combined sources4
Beta strandi233 – 242Combined sources10
Helixi248 – 255Combined sources8
Helixi261 – 264Combined sources4
Turni265 – 268Combined sources4
Helixi276 – 279Combined sources4
Helixi281 – 283Combined sources3
Beta strandi289 – 291Combined sources3
Beta strandi296 – 298Combined sources3
Helixi300 – 302Combined sources3
Helixi308 – 312Combined sources5
Turni314 – 316Combined sources3
Beta strandi321 – 329Combined sources9
Turni335 – 337Combined sources3
Beta strandi343 – 349Combined sources7
Helixi356 – 372Combined sources17
Helixi379 – 386Combined sources8
Helixi388 – 394Combined sources7
Helixi401 – 403Combined sources3
Beta strandi404 – 406Combined sources3
Helixi417 – 419Combined sources3
Helixi428 – 434Combined sources7

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP45574.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini294 – 3224Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd BLAST29

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)DescriptionActionsGraphical viewLength
Sequence conflicti22S → V AA sequence (PubMed:1555572).Curated1
Sequence conflicti26Q → K AA sequence (PubMed:1555572).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V4JX-ray2.10A/D1-437[»]
ProteinModelPortaliP45574.
SMRiP45574.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP45574. 4 interactors.
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

BioCyciMetaCyc: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: November 2, 2016
This is version 103 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.