Sulfite reductase, dissimilatory-type subunit beta - Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)

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P45575 (DSVB_DESVH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Sulfite reductase, dissimilatory-type subunit beta
EC=1.8.99.3

Alternative name(s):
Desulfoviridin subunit beta
Hydrogensulfite reductase subunit beta

Gene names

Name:	dsvB
Ordered Locus Names:	DVU_0403

Organism

Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) [Reference proteome] [HAMAP]

Taxonomic identifier

882 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio ›

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration, a process catalyzed by the sulfate-reducing bacteria.
Catalytic activity	(O₃S.S.SO₃)²- + acceptor + 2 H₂O + OH^- = 3 HSO₃^- + reduced acceptor.
Cofactor	Binds 1 4Fe-4S cluster per subunit. Binds 2 sirohemes per subunit.
Subunit structure	Heterohexamer of two alpha, two beta and two gamma subunits.
Sequence similarities	Contains 1 4Fe-4S ferredoxin-type domain.

Ontologies

Keywords
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	sulfur compound metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro hydrogensulfite reductase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 381

380

Sulfite reductase, dissimilatory-type subunit beta

PRO_0000080032

Regions

Domain

249 – 276

4Fe-4S ferredoxin-type

Sites

Metal binding

231

Iron-sulfur (4Fe-4S) Potential

Metal binding

258

Iron-sulfur (4Fe-4S) Potential

Metal binding

261

Iron-sulfur (4Fe-4S) Potential

Metal binding

264

Iron-sulfur (4Fe-4S) Potential

Secondary structure

381

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P45575 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 678A04F716050D63
Show »

FASTA

381

42,519

        10         20         30         40         50         60 
MAFISSGYNP EKPMANRITD IGPRKFDEFF PPVIAKNFGS WLYHEILEPG VLMHVAESGD 

        70         80         90        100        110        120 
KVYTVRVGAA RLMSITHIRE MCDIADKYCG GHLRFTTRNN VEFMVADEAS LKALKEDLAS 

       130        140        150        160        170        180 
RKFDGGSLKF PIGGTGAGVS NIVHTQGWVH CHTPATDASG PVKAIMDEVF EDFQSMRLPA 

       190        200        210        220        230        240 
PVRISLACCI NMCGAVHCSD IGVVGIHRKP PMIDHEWTDQ LCEIPLAVAS CPTAAVRPTK 

       250        260        270        280        290        300 
LEIGDKKVNT IAIKNERCMY CGNCYTMCPA LPISDGEGDG VVIMVGGKVS NRISMPKFSK 

       310        320        330        340        350        360 
VVVAYIPNEP PRWPSLTKTI KHIIEVYSAN AYKYERLGEW AERIGWERFF SLTGLEFSHH 

       370        380 
LIDDFRDPAY YTWRQSTQFK F

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conservation of the genes for dissimilatory sulfite reductase from Desulfovibrio vulgaris and Archaeoglobus fulgidus allows their detection by PCR." Karkhoff-Schweizer R.R., Huber D.P.W., Voordouw G. Appl. Environ. Microbiol. 61:290-296(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough." Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Fouts D.E. Fraser C.M. Nat. Biotechnol. 22:554-559(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hildenborough / ATCC 29579 / NCIMB 8303.
[3]	"The third subunit of desulfoviridin-type dissimilatory sulfite reductases." Pierik A.J., Duyvis M.G., van Helvoort J.M.L.M., Wolbert R.B.G., Hagen W.R. Eur. J. Biochem. 205:111-115(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U16723 Genomic DNA. Translation: AAA70108.1.
AE017285 Genomic DNA. Translation: AAS94886.1.

PIR

S21238.

RefSeq

YP_009627.1. NC_002937.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V4J	X-ray	2.10	B/E	1-381	[»]

ProteinModelPortal

P45575.

SMR

P45575. Positions 15-381.

ModBase

Search...

Protein-protein interaction databases

STRING

882.DVU0403.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAS94886; AAS94886; DVU_0403.

GeneID

2796153.

KEGG

dvu:DVU0403.

PATRIC

32060774. VBIDesVul119526_0380.

Phylogenomic databases

eggNOG

COG2221.

K11181.

OMA

WLHCDIP.

ProtClustDB

CLSK862601.

Enzyme and pathway databases

BioCyc

DVUL882:GJIL-423-MONOMER.
MetaCyc:MONOMER-12512.

BRENDA

1.8.99.3. 1914.

Family and domain databases

InterPro

IPR017896. 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]

Pfam

PF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 1 hit.
[Graphical view]

SUPFAM

SSF55124. NiR_SiRalpha_1/3. 1 hit.

TIGRFAMs

TIGR02066. dsrB. 1 hit.

PROSITE

PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P45575.

Entry information

Entry name

DSVB_DESVH

Accession

Primary (citable) accession number: P45575

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents