MBHJ_PYRFU
ID MBHJ_PYRFU Reviewed; 167 AA.
AC Q8U0Z8;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable membrane-bound hydrogenase subunit mbhJ {ECO:0000303|PubMed:10852873};
DE EC=1.12.7.2 {ECO:0000269|PubMed:10852873};
GN Name=mbhJ {ECO:0000303|PubMed:11054105};
GN Synonyms=mbh10 {ECO:0000303|PubMed:10852873}; OrderedLocusNames=PF1432;
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:AAL81556.1}
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP 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 [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, SUBCELLULAR LOCATION, AND EPR 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 [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: Probable subunit of a hydrogen-evolving hydrogenase that
CC utilizes 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
CC membrane, 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:10852873};
CC Note=Binds 1 [4Fe-4S] cluster. {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, but 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 20 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}.
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DR EMBL; AE009950; AAL81556.1; -; Genomic_DNA.
DR RefSeq; WP_011012579.1; NZ_CP023154.1.
DR PDB; 6CFW; EM; 3.70 A; J=1-167.
DR PDBsum; 6CFW; -.
DR AlphaFoldDB; Q8U0Z8; -.
DR SMR; Q8U0Z8; -.
DR STRING; 186497.PF1432; -.
DR TCDB; 3.D.1.4.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; AAL81556; AAL81556; PF1432.
DR GeneID; 41713241; -.
DR KEGG; pfu:PF1432; -.
DR PATRIC; fig|186497.12.peg.1494; -.
DR eggNOG; arCOG01553; Archaea.
DR HOGENOM; CLU_055737_7_3_2; -.
DR OMA; WVFHVNS; -.
DR OrthoDB; 100307at2157; -.
DR PhylomeDB; Q8U0Z8; -.
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:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:UniProtKB.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR Pfam; PF01058; Oxidored_q6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..167
FT /note="Probable membrane-bound hydrogenase subunit mbhJ"
FT /id="PRO_0000420790"
FT BINDING 35
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P21853"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P21853"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P21853"
FT BINDING 132
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P21853"
SQ SEQUENCE 167 AA; 18302 MW; B129066FC12465C9 CRC64;
MTNNSERKRL EKRIAQLCKF IGRSPWVFHV NSGSCNGCDI EIIAALTPRY DAERFGVKLV
GSPRHADILL VTGPVTNQSL ERVKLVYEQT PDPKIVIAIG ACPTGGSVFY ESPFTNAPLD
RIIPVDVFVP GCPPRPEAIL HGVVLALEKL AKMIKGEVPP EEGEENE
