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Protein

Membrane-bound hydrogenase subunit alpha

Gene

mbhL

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

Alpha subunit of a hydrogen-evolving hydrogenase that utilizes protons both as a substrate for hydrogen production and proton translocation. Acts by coupling the redox reaction via ferredoxin and iron-sulfur (Fe-S) clusters to proton translocation across the membane thereby conserving the redox energy in a proton gradient.3 Publications

Catalytic activityi

H2 + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H+.3 Publications

Cofactori

Ni2+1 PublicationNote: Binds 1 nickel ion per mole of protein.1 Publication

Enzyme regulationi

Inhibited by 0.1 mM Cu2+.1 Publication

Kineticsi

Measured for the whole complex.1 Publication

  1. KM=36 µM for ferredoxin2 Publications

    pH dependencei

    Optimum pH is 7.0. Active between pH 6.0-8.5.2 Publications

    Temperature dependencei

    Optimum temperature is 90 degrees Celsius for membrane-bound enzyme but 80 degrees Celsius for the purified enzyme. Membrane-bound enzyme has a half-life of 2h at 100 degrees Celsius whereas the half-life of the purified enzyme is 30 minutes at 100 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi68 – 681NickelBy similarity
    Metal bindingi71 – 711NickelBy similarity
    Metal bindingi374 – 3741NickelBy similarity
    Metal bindingi377 – 3771NickelBy similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, Nickel

    Enzyme and pathway databases

    BRENDAi1.12.7.2. 5243.

    Protein family/group databases

    TCDBi3.D.1.4.1. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Membrane-bound hydrogenase subunit alpha1 Publication (EC:1.12.7.21 Publication)
    Short name:
    MBH-alpha1 Publication
    Gene namesi
    Name:mbhL1 Publication
    Synonyms:mbh121 Publication
    Ordered Locus Names:PF1434
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    Proteomesi
    • UP000001013 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 427427Membrane-bound hydrogenase subunit alphaPRO_0000420791Add
    BLAST

    Proteomic databases

    PRIDEiQ8U0Z6.

    Interactioni

    Subunit structurei

    The membrane-bound hydrogenase complex is composed of MbhK and MbhL, and may also contain MbhJ.1 Publication

    Protein-protein interaction databases

    STRINGi186497.PF1434.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8U0Z6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the complex I 49 kDa subunit family.Curated

    Phylogenomic databases

    eggNOGiarCOG01547. Archaea.
    COG3261. LUCA.
    HOGENOMiHOG000228263.
    KOiK18016.
    OMAiASESHFD.

    Family and domain databases

    Gene3Di1.10.645.10. 2 hits.
    InterProiIPR001135. NADH_Q_OxRdtase_suD.
    IPR001501. Ni-dep_hyd_lsu.
    IPR029014. NiFe_Hase-like.
    [Graphical view]
    PfamiPF00346. Complex1_49kDa. 1 hit.
    PF00374. NiFeSe_Hases. 1 hit.
    [Graphical view]
    SUPFAMiSSF56762. SSF56762. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8U0Z6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKKVEYWVKI PFGPIHPGLE EPEKFIITLD GERIVNVDVK LGYNLRGVQW
    60 70 80 90 100
    IGMRRNYVQI MYLAERMCGI CSFSHNHTYV RAVEEMAGIE VPERAEYIRV
    110 120 130 140 150
    IVGELERIHS HLLNLGVVGH DIGYDTVLHL TWLARERVMD VLEAVSGNRV
    160 170 180 190 200
    NYSMVTIGGV RRDIGEKQKR LILDMIKYYR EVLPQIEDVF LHDSTIEARL
    210 220 230 240 250
    RDVAVVPKKL AIEMGAVGPT ARGSGIKEDS RWSEQLGVYP DLGIKPVTPE
    260 270 280 290 300
    DVTGEKARGD VYDRMAVRIG ELWMSLDLLE HALDQMPEGK IKTFPKDNIL
    310 320 330 340 350
    VAKLKLLGDG EGIGRYEAPR GELVHYVRGQ KGRDGPVRWK PREPTFPNLF
    360 370 380 390 400
    TIAKALEGNE LADLVVAIAS IDPCLSCTDR VAIVKEGKKV VLTEKDLLKL
    410 420
    SIEKTKEINP NVKGDPTPTG IGCSRGV
    Length:427
    Mass (Da):47,934
    Last modified:June 1, 2002 - v1
    Checksum:iC7083303E5502B92
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009950 Genomic DNA. Translation: AAL81558.1.
    RefSeqiWP_011012581.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL81558; AAL81558; PF1434.
    GeneIDi1469310.
    KEGGipfu:PF1434.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009950 Genomic DNA. Translation: AAL81558.1.
    RefSeqiWP_011012581.1. NC_003413.1.

    3D structure databases

    ProteinModelPortaliQ8U0Z6.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi186497.PF1434.

    Protein family/group databases

    TCDBi3.D.1.4.1. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

    Proteomic databases

    PRIDEiQ8U0Z6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL81558; AAL81558; PF1434.
    GeneIDi1469310.
    KEGGipfu:PF1434.

    Phylogenomic databases

    eggNOGiarCOG01547. Archaea.
    COG3261. LUCA.
    HOGENOMiHOG000228263.
    KOiK18016.
    OMAiASESHFD.

    Enzyme and pathway databases

    BRENDAi1.12.7.2. 5243.

    Family and domain databases

    Gene3Di1.10.645.10. 2 hits.
    InterProiIPR001135. NADH_Q_OxRdtase_suD.
    IPR001501. Ni-dep_hyd_lsu.
    IPR029014. NiFe_Hase-like.
    [Graphical view]
    PfamiPF00346. Complex1_49kDa. 1 hit.
    PF00374. NiFeSe_Hases. 1 hit.
    [Graphical view]
    SUPFAMiSSF56762. SSF56762. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "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.
    2. Cited for: PROTEIN SEQUENCE OF 1-30, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, EPR SPECTROSCOPY.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc11 Publication.
    3. "Purification and characterization of a membrane-bound hydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus."
      Sapra R., Verhagen M.F., Adams M.W.
      J. Bacteriol. 182:3423-3428(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, EPR SPECTROSCOPY.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc11 Publication.
    4. "A simple energy-conserving system: proton reduction coupled to proton translocation."
      Sapra R., Bagramyan K., Adams M.W.
      Proc. Natl. Acad. Sci. U.S.A. 100:7545-7550(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc11 Publication.

    Entry informationi

    Entry nameiMBHLA_PYRFU
    AccessioniPrimary (citable) accession number: Q8U0Z6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 9, 2013
    Last sequence update: June 1, 2002
    Last modified: November 11, 2015
    This is version 80 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    The subunit composition of membrane-bound hydrogenase complex is currently unclear. It has been shown to be a heterodimer of MbhK and MbhL (PubMed:10852873). Other studies have shown it to contain MbhJ in addition to MbhK and MbhL (PubMed:11054105).2 Publications

    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.