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Protein

Sulfhydrogenase 1 subunit beta

Gene

hydB

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Part of a bifunctional enzyme complex that functions as an NADPH-dependent hydrogen-evolving hydrogenase with sulfur reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity not exhibited with NAD. The beta and gamma subunits form the sulfur reducing component that catalyzes the cytoplasmic production of hydrogen sulfide in the presence of elemental sulfur. Not active in the presence of sodium sulfate, sodium sulfite, sodium thiosulfate or cysteine.4 Publications

Catalytic activityi

H2 + polysulfide(n) = hydrogen sulfide + polysulfide(n-1).2 Publications

Cofactori

[4Fe-4S] cluster2 PublicationsNote: Binds 2 [4Fe-4S] clusters.2 Publications

Enzyme regulationi

Stimulated by rubredoxin at pH 7.6 but not ferredoxin.1 Publication

Kineticsi

Measured for the whole complex.1 Publication

    1. Vmax=6 µmol/min/mg enzyme2 Publications

    pH dependencei

    Optimum pH is 8.4 for sulfur reductase activity at 80 degrees Celsius.2 Publications

    Temperature dependencei

    Optimum temperature is 80 degrees Celsius for maximal sulfur reductase activity. Activity increases linearly from above 30 degrees Celsius to reach maximal levels at 80 degrees Celsius and then decreases to 15% of activity at 90 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi233 – 2331Iron-sulfur 1 (4Fe-4S)By similarity
    Metal bindingi236 – 2361Iron-sulfur 1 (4Fe-4S)By similarity
    Metal bindingi239 – 2391Iron-sulfur 1 (4Fe-4S)By similarity
    Metal bindingi243 – 2431Iron-sulfur 1 (4Fe-4S)By similarity
    Metal bindingi312 – 3121Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi315 – 3151Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi318 – 3181Iron-sulfur 2 (4Fe-4S)By similarity
    Metal bindingi322 – 3221Iron-sulfur 2 (4Fe-4S)By similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi1.12.98.4. 5243.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfhydrogenase 1 subunit beta (EC:1.12.98.4)
    Alternative name(s):
    Sulfhydrogenase I subunit beta1 Publication
    Sulfur reductase subunit HydB1 Publication
    Gene namesi
    Name:hydB1 Publication
    Ordered Locus Names:PF0891
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    Proteomesi
    • UP000001013 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm 2 Publications

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 367367Sulfhydrogenase 1 subunit betaPRO_0000420723Add
    BLAST

    Interactioni

    Subunit structurei

    Heterotetramer of alpha, beta, gamma and delta subunits. The nickel-containing alpha and delta subunits constitute the hydrogenase activity. The beta and gamma subunits (flavin-containing dimer) constitute the sulfur reductase activity.3 Publications

    Protein-protein interaction databases

    STRINGi186497.PF0891.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8U2E5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini222 – 254334Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini303 – 332304Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiarCOG05128. Archaea.
    COG1145. LUCA.
    HOGENOMiHOG000227558.
    KOiK17996.
    OMAiRWRQRIM.

    Family and domain databases

    InterProiIPR017896. 4Fe4S_Fe-S-bd.
    IPR017900. 4Fe4S_Fe_S_CS.
    [Graphical view]
    PfamiPF17179. Fer4_22. 1 hit.
    [Graphical view]
    PROSITEiPS00198. 4FE4S_FER_1. 2 hits.
    PS51379. 4FE4S_FER_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8U2E5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRYVKLPKEN TYEFLERLKD WGKLYAPVKI SDKFYDFREI DDVRKIEFHY
    60 70 80 90 100
    NRTIMPPKKF FFKPREKLFE FDISKPEYRE VIEEVEPFII FGVHACDIYG
    110 120 130 140 150
    LKILDTVYLD EFPDKYYKVR REKGIIIGIS CMPDEYCFCN LRETDFADDG
    160 170 180 190 200
    FDLFFHELPD GWLVRVGTPT GHRLVDKNIK LFEEVTDKDI CAFRDFEKRR
    210 220 230 240 250
    QQAFKYHEDW GNLRYLLELE MEHPMWDEEA DKCLACGICN TTCPTCRCYE
    260 270 280 290 300
    VQDIVNLDGV TGYRERRWDS CQFRSHGLVA GGHNFRPTKK DRFRNRYLCK
    310 320 330 340 350
    NAYNEKLGLS YCVGCGRCTA FCPANISFVG NLRRILGLEE NKCPPTVSEE
    360
    IPKRGFAYSS NIRGDGV
    Length:367
    Mass (Da):43,399
    Last modified:June 1, 2002 - v1
    Checksum:i8329F3842CBC48D0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti205 – 2051K → Q in CAA53034 (PubMed:7704275).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X75255 Genomic DNA. Translation: CAA53034.1.
    AE009950 Genomic DNA. Translation: AAL81015.1.
    RefSeqiWP_011012026.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL81015; AAL81015; PF0891.
    GeneIDi1468753.
    KEGGipfu:PF0891.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X75255 Genomic DNA. Translation: CAA53034.1.
    AE009950 Genomic DNA. Translation: AAL81015.1.
    RefSeqiWP_011012026.1. NC_003413.1.

    3D structure databases

    ProteinModelPortaliQ8U2E5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi186497.PF0891.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL81015; AAL81015; PF0891.
    GeneIDi1468753.
    KEGGipfu:PF0891.

    Phylogenomic databases

    eggNOGiarCOG05128. Archaea.
    COG1145. LUCA.
    HOGENOMiHOG000227558.
    KOiK17996.
    OMAiRWRQRIM.

    Enzyme and pathway databases

    BRENDAi1.12.98.4. 5243.

    Family and domain databases

    InterProiIPR017896. 4Fe4S_Fe-S-bd.
    IPR017900. 4Fe4S_Fe_S_CS.
    [Graphical view]
    PfamiPF17179. Fer4_22. 1 hit.
    [Graphical view]
    PROSITEiPS00198. 4FE4S_FER_1. 2 hits.
    PS51379. 4FE4S_FER_2. 2 hits.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Characterization of the locus encoding the [Ni-Fe] sulfhydrogenase from the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial sulfite reductases."
      Pedroni P., Della Volpe A., Galli G., Mura G.M., Pratesi C., Grandi G.
      Microbiology 141:449-458(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc11 Publication.
    2. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
      Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
      Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    3. "Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor."
      Ma K., Schicho R.N., Kelly R.M., Adams M.W.
      Proc. Natl. Acad. Sci. U.S.A. 90:5341-5344(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBUNIT.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc11 Publication.
    4. "Redox properties of the sulfhydrogenase from Pyrococcus furiosus."
      Arendsen A.F., Veenhuizen P.T., Hagen W.R.
      FEBS Lett. 368:117-121(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, EPR SPECTROSCOPY.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc11 Publication.
    5. "On the prosthetic groups of the NiFe sulfhydrogenase from Pyrococcus furiosus: topology, structure, and temperature-dependent redox chemistry."
      Silva P.J., de Castro B., Hagen W.R.
      J. Biol. Inorg. Chem. 4:284-291(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR, EPR SPECTROSCOPY.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc11 Publication.
    6. "Hydrogenases I and II from Pyrococcus furiosus."
      Ma K., Adams M.W.
      Methods Enzymol. 331:208-216(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc11 Publication.

    Entry informationi

    Entry nameiHYD1B_PYRFU
    AccessioniPrimary (citable) accession number: Q8U2E5
    Secondary accession number(s): Q59667
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2013
    Last sequence update: June 1, 2002
    Last modified: May 11, 2016
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. 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.