MBHLB_PYRFU
ID MBHLB_PYRFU Reviewed; 173 AA.
AC Q8U0Z7;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Membrane-bound hydrogenase subunit beta {ECO:0000303|PubMed:10852873};
DE EC=1.12.7.2 {ECO:0000269|PubMed:10852873};
GN Name=mbhK {ECO:0000303|PubMed:11054105};
GN Synonyms=mbh11 {ECO:0000303|PubMed:10852873}; OrderedLocusNames=PF1433;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1] {ECO:0000312|EMBL:AAL81557.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND EPR
RP SPECTROSCOPY.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000269|PubMed:10852873};
RX PubMed=10852873; DOI=10.1128/jb.182.12.3423-3428.2000;
RA Sapra R., Verhagen M.F., Adams M.W.;
RT "Purification and characterization of a membrane-bound hydrogenase from the
RT hyperthermophilic archaeon Pyrococcus furiosus.";
RL J. Bacteriol. 182:3423-3428(2000).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 3-25, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND EPR SPECTROSCOPY.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000269|PubMed:11054105};
RX PubMed=11054105; DOI=10.1046/j.1432-1327.2000.01745.x;
RA Silva P.J., van den Ban E.C., Wassink H., Haaker H., de Castro B.,
RA Robb F.T., Hagen W.R.;
RT "Enzymes of hydrogen metabolism in Pyrococcus furiosus.";
RL Eur. J. Biochem. 267:6541-6551(2000).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000269|PubMed:12792025};
RX PubMed=12792025; DOI=10.1073/pnas.1331436100;
RA Sapra R., Bagramyan K., Adams M.W.;
RT "A simple energy-conserving system: proton reduction coupled to proton
RT translocation.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7545-7550(2003).
CC -!- FUNCTION: Beta subunit of a hydrogen-evolving hydrogenase that utilizes
CC protons both as a substrate for hydrogen production and proton
CC translocation. Acts by coupling the redox reaction via ferredoxin and
CC iron-sulfur (Fe-S) clusters to proton translocation across the membrane
CC thereby conserving the redox energy in a proton gradient.
CC {ECO:0000269|PubMed:10852873, ECO:0000269|PubMed:11054105,
CC ECO:0000269|PubMed:12792025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2 + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H(+) + 2 reduced
CC [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:17445, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.12.7.2;
CC Evidence={ECO:0000269|PubMed:10852873, ECO:0000269|PubMed:11054105,
CC ECO:0000269|PubMed:12792025};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:10852873};
CC Note=Binds 1 nickel ion per mole of protein.
CC {ECO:0000269|PubMed:10852873};
CC -!- ACTIVITY REGULATION: Inhibited by 0.1 mM Cu(2+).
CC {ECO:0000269|PubMed:12792025}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for ferredoxin {ECO:0000269|PubMed:10852873,
CC ECO:0000269|PubMed:11054105};
CC Note=Measured for the whole complex. {ECO:0000269|PubMed:11054105};
CC pH dependence:
CC Optimum pH is 7.0. Active between pH 6.0-8.5.
CC {ECO:0000269|PubMed:10852873, ECO:0000269|PubMed:11054105};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius for membrane-bound enzyme
CC but 80 degrees Celsius for the purified enzyme. Membrane-bound enzyme
CC has a half-life of 2h at 100 degrees Celsius whereas the half-life of
CC the purified enzyme is 30 minutes at 100 degrees Celsius.
CC {ECO:0000269|PubMed:10852873, ECO:0000269|PubMed:11054105};
CC -!- SUBUNIT: The membrane-bound hydrogenase complex is composed of MbhK and
CC MbhL, and may also contain MbhJ. {ECO:0000269|PubMed:10852873}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10852873,
CC ECO:0000269|PubMed:11054105}.
CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC {ECO:0000305}.
CC -!- CAUTION: The subunit composition of membrane-bound hydrogenase complex
CC is currently unclear. It has been shown to be a heterodimer of MbhK and
CC MbhL (PubMed:10852873). Other studies have shown it to contain MbhJ in
CC addition to MbhK and MbhL (PubMed:11054105).
CC {ECO:0000305|PubMed:10852873, ECO:0000305|PubMed:11054105}.
CC -!- CAUTION: There is conflicting N-terminal sequencing data for this
CC protein. The mature protein may start from Ser-2 (PubMed:10852873) or
CC Lys-3 (PubMed:11054105). {ECO:0000305, ECO:0000305|PubMed:10852873,
CC ECO:0000305|PubMed:11054105}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE009950; AAL81557.1; -; Genomic_DNA.
DR RefSeq; WP_011012580.1; NZ_CP023154.1.
DR PDB; 6CFW; EM; 3.70 A; K=1-173.
DR PDBsum; 6CFW; -.
DR AlphaFoldDB; Q8U0Z7; -.
DR SMR; Q8U0Z7; -.
DR STRING; 186497.PF1433; -.
DR TCDB; 3.D.1.4.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PRIDE; Q8U0Z7; -.
DR DNASU; 1469309; -.
DR EnsemblBacteria; AAL81557; AAL81557; PF1433.
DR GeneID; 41713242; -.
DR KEGG; pfu:PF1433; -.
DR PATRIC; fig|186497.12.peg.1495; -.
DR eggNOG; arCOG01552; Archaea.
DR HOGENOM; CLU_097415_1_0_2; -.
DR OMA; HYSIGIE; -.
DR OrthoDB; 101801at2157; -.
DR PhylomeDB; Q8U0Z7; -.
DR BRENDA; 1.12.7.2; 5243.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0009375; C:ferredoxin hydrogenase complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:UniProtKB.
DR Gene3D; 3.30.460.80; -; 1.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR SUPFAM; SSF143243; SSF143243; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Membrane;
KW Metal-binding; Nickel; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10852873"
FT CHAIN 2..173
FT /note="Membrane-bound hydrogenase subunit beta"
FT /evidence="ECO:0000269|PubMed:10852873"
FT /id="PRO_0000420792"
FT CONFLICT 23..24
FT /note="KT -> GD (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000269|PubMed:11054105"
SQ SEQUENCE 173 AA; 20184 MW; E3BBD74C5B7E0593 CRC64;
MSKAEMVANK IKERFPNAEV VVKTNKWGRE RVWVRISREE YKELMKFIRE LDPEAHYSIG
IEQDWGDELG FLNHILLFYD EPPGVSLLID VHAPKDNPVL PDTSDIFPIS LQFEREGMEM
VGLDFEGAPD KRRLFLPDDF PEGIYPLRTD EKGVPEEMVK NAGHPYLLRR EKK
