MBHLA_PYRFU
ID MBHLA_PYRFU Reviewed; 427 AA.
AC Q8U0Z6;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Membrane-bound hydrogenase subunit alpha {ECO:0000303|PubMed:10852873};
DE Short=MBH-alpha {ECO:0000303|PubMed:10852873};
DE EC=1.12.7.2 {ECO:0000269|PubMed:10852873};
GN Name=mbhL {ECO:0000303|PubMed:11054105};
GN Synonyms=mbh12 {ECO:0000303|PubMed:10852873}; OrderedLocusNames=PF1434;
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:AAL81558.1}
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 1-30, 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 [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-10, 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 [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: Alpha 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 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 49 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; AAL81558.1; -; Genomic_DNA.
DR RefSeq; WP_011012581.1; NZ_CP023154.1.
DR PDB; 6CFW; EM; 3.70 A; L=1-380.
DR PDBsum; 6CFW; -.
DR AlphaFoldDB; Q8U0Z6; -.
DR SMR; Q8U0Z6; -.
DR STRING; 186497.PF1434; -.
DR TCDB; 3.D.1.4.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; AAL81558; AAL81558; PF1434.
DR GeneID; 41713243; -.
DR KEGG; pfu:PF1434; -.
DR PATRIC; fig|186497.12.peg.1496; -.
DR eggNOG; arCOG01547; Archaea.
DR HOGENOM; CLU_015134_1_2_2; -.
DR OMA; ICSFSHN; -.
DR OrthoDB; 4328at2157; -.
DR PhylomeDB; Q8U0Z6; -.
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:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IDA:UniProtKB.
DR Gene3D; 1.10.645.10; -; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR001501; Ni-dep_hyd_lsu.
DR InterPro; IPR029014; NiFe-Hase_large.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR Pfam; PF00374; NiFeSe_Hases; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Membrane;
KW Metal-binding; Nickel; Oxidoreductase; Reference proteome.
FT CHAIN 1..427
FT /note="Membrane-bound hydrogenase subunit alpha"
FT /id="PRO_0000420791"
FT BINDING 68
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250|UniProtKB:P12944"
FT BINDING 71
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250|UniProtKB:P12944"
FT BINDING 374
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250|UniProtKB:P12944"
FT BINDING 377
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250|UniProtKB:P12944"
SQ SEQUENCE 427 AA; 47934 MW; C7083303E5502B92 CRC64;
MKKVEYWVKI PFGPIHPGLE EPEKFIITLD GERIVNVDVK LGYNLRGVQW IGMRRNYVQI
MYLAERMCGI CSFSHNHTYV RAVEEMAGIE VPERAEYIRV IVGELERIHS HLLNLGVVGH
DIGYDTVLHL TWLARERVMD VLEAVSGNRV NYSMVTIGGV RRDIGEKQKR LILDMIKYYR
EVLPQIEDVF LHDSTIEARL RDVAVVPKKL AIEMGAVGPT ARGSGIKEDS RWSEQLGVYP
DLGIKPVTPE DVTGEKARGD VYDRMAVRIG ELWMSLDLLE HALDQMPEGK IKTFPKDNIL
VAKLKLLGDG EGIGRYEAPR GELVHYVRGQ KGRDGPVRWK PREPTFPNLF TIAKALEGNE
LADLVVAIAS IDPCLSCTDR VAIVKEGKKV VLTEKDLLKL SIEKTKEINP NVKGDPTPTG
IGCSRGV
