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Protein

Sulfite reductase, dissimilatory-type subunit beta

Gene

dsvB

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
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, a process catalyzed by the sulfate-reducing bacteria.2 Publications

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:
  • [4Fe-4S] cluster1 PublicationNote: Binds 2 [4Fe-4S] clusters per subunit.1 Publication
  • siroheme1 PublicationNote: Binds 1 siroheme per subunit.1 Publication

Kineticsi

kcat is 0.31 (sec-1) for sulfite. kcat is 0.038 (sec-1) for nitrite.1 Publication

Manual assertion based on experiment ini

  1. KM=0.06 mM for sulfite1 Publication
  2. KM=0.028 mM for nitrite1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi151Iron-sulfur (4Fe-4S) 1Combined sources1 Publication1
    Metal bindingi188Iron-sulfur (4Fe-4S) 1Combined sources1 Publication1
    Metal bindingi189Iron-sulfur (4Fe-4S) 1Combined sources1 Publication1
    Metal bindingi193Iron (siroheme axial ligand)1 Publication1
    Metal bindingi193Iron-sulfur (4Fe-4S) 1Combined sources1 Publication1
    Metal bindingi231Iron-sulfur (4Fe-4S) 2Combined sources1 Publication1
    Metal bindingi258Iron-sulfur (4Fe-4S) 2Combined sources1 Publication1
    Metal bindingi261Iron-sulfur (4Fe-4S) 2Combined sources1 Publication1
    Metal bindingi264Iron-sulfur (4Fe-4S) 2Combined sources1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12512.
    BRENDAi1.8.99.3. 1914.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfite reductase, dissimilatory-type subunit beta (EC:1.8.99.52 Publications)
    Alternative name(s):
    Desulfoviridin subunit beta1 Publication
    Dissimilatory sulfite reductase subunit beta1 Publication
    Short name:
    dSiR beta1 Publication
    Hydrogensulfite reductase subunit beta
    Gene namesi
    Name:dsvB
    Synonyms:dsrB1 Publication
    Ordered Locus Names:DVU_0403
    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_00000800322 – 381Sulfite reductase, dissimilatory-type subunit betaAdd BLAST380

    Proteomic databases

    PaxDbiP45575.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiP45575. 2 interactors.
    STRINGi882.DVU0403.

    Structurei

    Secondary structure

    1381
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni13 – 16Combined sources4
    Turni26 – 29Combined sources4
    Helixi32 – 37Combined sources6
    Beta strandi41 – 48Combined sources8
    Beta strandi51 – 56Combined sources6
    Beta strandi61 – 67Combined sources7
    Beta strandi71 – 74Combined sources4
    Helixi75 – 88Combined sources14
    Beta strandi92 – 95Combined sources4
    Beta strandi101 – 107Combined sources7
    Helixi108 – 120Combined sources13
    Beta strandi128 – 130Combined sources3
    Beta strandi136 – 139Combined sources4
    Helixi147 – 149Combined sources3
    Helixi159 – 173Combined sources15
    Beta strandi178 – 180Combined sources3
    Beta strandi184 – 189Combined sources6
    Helixi196 – 198Combined sources3
    Beta strandi199 – 206Combined sources8
    Helixi215 – 221Combined sources7
    Helixi224 – 229Combined sources6
    Beta strandi236 – 243Combined sources8
    Beta strandi246 – 253Combined sources8
    Helixi255 – 257Combined sources3
    Helixi263 – 267Combined sources5
    Turni276 – 278Combined sources3
    Beta strandi280 – 285Combined sources6
    Beta strandi292 – 294Combined sources3
    Beta strandi300 – 307Combined sources8
    Turni310 – 312Combined sources3
    Helixi314 – 330Combined sources17
    Helixi337 – 344Combined sources8
    Helixi346 – 353Combined sources8
    Helixi359 – 361Combined sources3
    Helixi367 – 372Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2V4JX-ray2.10B/E1-381[»]
    ProteinModelPortaliP45575.
    SMRiP45575.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45575.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini249 – 2764Fe-4S ferredoxin-typePROSITE-ProRule annotationAdd BLAST28

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiENOG4105PJW. Bacteria.
    COG2221. LUCA.
    KOiK11181.
    OMAiWLHCDIP.
    OrthoDBiPOG091H10MD.

    Family and domain databases

    InterProiIPR017896. 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]
    PfamiPF01077. NIR_SIR. 1 hit.
    PF03460. NIR_SIR_ferr. 1 hit.
    [Graphical view]
    SUPFAMiSSF55124. SSF55124. 1 hit.
    TIGRFAMsiTIGR02066. dsrB. 1 hit.
    PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
    PS51379. 4FE4S_FER_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P45575-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAFISSGYNP EKPMANRITD IGPRKFDEFF PPVIAKNFGS WLYHEILEPG
    60 70 80 90 100
    VLMHVAESGD KVYTVRVGAA RLMSITHIRE MCDIADKYCG GHLRFTTRNN
    110 120 130 140 150
    VEFMVADEAS LKALKEDLAS RKFDGGSLKF PIGGTGAGVS NIVHTQGWVH
    160 170 180 190 200
    CHTPATDASG PVKAIMDEVF EDFQSMRLPA PVRISLACCI NMCGAVHCSD
    210 220 230 240 250
    IGVVGIHRKP PMIDHEWTDQ LCEIPLAVAS CPTAAVRPTK LEIGDKKVNT
    260 270 280 290 300
    IAIKNERCMY CGNCYTMCPA LPISDGEGDG VVIMVGGKVS NRISMPKFSK
    310 320 330 340 350
    VVVAYIPNEP PRWPSLTKTI KHIIEVYSAN AYKYERLGEW AERIGWERFF
    360 370 380
    SLTGLEFSHH LIDDFRDPAY YTWRQSTQFK F
    Length:381
    Mass (Da):42,519
    Last modified:January 23, 2007 - v3
    Checksum:i678A04F716050D63
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U16723 Genomic DNA. Translation: AAA70108.1.
    AE017285 Genomic DNA. Translation: AAS94886.1.
    PIRiS21238.
    RefSeqiWP_010937710.1. NC_002937.3.
    YP_009627.1. NC_002937.3.

    Genome annotation databases

    EnsemblBacteriaiAAS94886; AAS94886; DVU_0403.
    GeneIDi2796153.
    KEGGidvu:DVU0403.
    PATRICi32060774. VBIDesVul119526_0380.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U16723 Genomic DNA. Translation: AAA70108.1.
    AE017285 Genomic DNA. Translation: AAS94886.1.
    PIRiS21238.
    RefSeqiWP_010937710.1. NC_002937.3.
    YP_009627.1. NC_002937.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2V4JX-ray2.10B/E1-381[»]
    ProteinModelPortaliP45575.
    SMRiP45575.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP45575. 2 interactors.
    STRINGi882.DVU0403.

    Proteomic databases

    PaxDbiP45575.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAS94886; AAS94886; DVU_0403.
    GeneIDi2796153.
    KEGGidvu:DVU0403.
    PATRICi32060774. VBIDesVul119526_0380.

    Phylogenomic databases

    eggNOGiENOG4105PJW. Bacteria.
    COG2221. LUCA.
    KOiK11181.
    OMAiWLHCDIP.
    OrthoDBiPOG091H10MD.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-12512.
    BRENDAi1.8.99.3. 1914.

    Miscellaneous databases

    EvolutionaryTraceiP45575.

    Family and domain databases

    InterProiIPR017896. 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]
    PfamiPF01077. NIR_SIR. 1 hit.
    PF03460. NIR_SIR_ferr. 1 hit.
    [Graphical view]
    SUPFAMiSSF55124. SSF55124. 1 hit.
    TIGRFAMsiTIGR02066. dsrB. 1 hit.
    PROSITEiPS00198. 4FE4S_FER_1. 1 hit.
    PS51379. 4FE4S_FER_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDSVB_DESVH
    AccessioniPrimary (citable) accession number: P45575
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 109 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.