HYD2A_PYRFU
ID HYD2A_PYRFU Reviewed; 412 AA.
AC E7FHC4; Q7LWY6; Q9P9M4;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Sulfhydrogenase 2 subunit alpha;
DE EC=1.12.1.5;
DE AltName: Full=Hydrogen dehydrogenase (NAD(P)(+));
DE AltName: Full=Hydrogenase-II subunit alpha {ECO:0000303|PubMed:10714990};
DE Short=H-II alpha {ECO:0000303|PubMed:10714990};
DE AltName: Full=NADP-reducing hydrogenase subunit ShyA;
DE AltName: Full=Sulfhydrogenase II subunit alpha {ECO:0000303|PubMed:10714990};
GN Name=shyA {ECO:0000312|EMBL:AAF61854.1}; OrderedLocusNames=PF1332;
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:0000305, ECO:0000312|EMBL:AAF61854.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, SUBUNIT, AND EPR SPECTROSCOPY.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000312|EMBL:AAF61854.1};
RX PubMed=10714990; DOI=10.1128/jb.182.7.1864-1871.2000;
RA Ma K., Weiss R., Adams M.W.;
RT "Characterization of hydrogenase II from the hyperthermophilic archaeon
RT Pyrococcus furiosus and assessment of its role in sulfur reduction.";
RL J. Bacteriol. 182:1864-1871(2000).
RN [2] {ECO:0000312|EMBL:AAL81456.1}
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 [3] {ECO:0000305}
RP FUNCTION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000269|PubMed:11133967};
RX PubMed=11133967; DOI=10.1128/jb.183.2.716-724.2001;
RA Adams M.W., Holden J.F., Menon A.L., Schut G.J., Grunden A.M., Hou C.,
RA Hutchins A.M., Jenney F.E. Jr., Kim C., Ma K., Pan G., Roy R., Sapra R.,
RA Story S.V., Verhagen M.F.;
RT "Key role for sulfur in peptide metabolism and in regulation of three
RT hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus.";
RL J. Bacteriol. 183:716-724(2001).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000269|PubMed:11265463};
RX PubMed=11265463; DOI=10.1016/s0076-6879(01)31059-5;
RA Ma K., Adams M.W.;
RT "Hydrogenases I and II from Pyrococcus furiosus.";
RL Methods Enzymol. 331:208-216(2001).
CC -!- FUNCTION: Part of a bifunctional enzyme complex that functions as a
CC hydrogen-evolving hydrogenase with sulfur-reducing activity. May play a
CC role in hydrogen cycling during fermentative growth. Activity exhibited
CC with NAD in addition to NADPH. The alpha and delta subunits form the
CC hydrogenase component that catalyzes the reduction of protons to evolve
CC hydrogen. {ECO:0000269|PubMed:10714990, ECO:0000269|PubMed:11133967,
CC ECO:0000269|PubMed:11265463}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2 + NADP(+) = H(+) + NADPH; Xref=Rhea:RHEA:18637,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.12.1.5;
CC Evidence={ECO:0000269|PubMed:10714990, ECO:0000269|PubMed:11265463};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2 + NAD(+) = H(+) + NADH; Xref=Rhea:RHEA:24636,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.12.1.5;
CC Evidence={ECO:0000269|PubMed:10714990, ECO:0000269|PubMed:11265463};
CC -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:10714990};
CC Note=Binds 1 nickel ion per subunit. {ECO:0000269|PubMed:10714990};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.25 mM for methyl viologen (sodium dithionate and H(+) as
CC cosubstrates) {ECO:0000269|PubMed:10714990};
CC KM=1.0 mM for methyl viologen (H(2) as cosubstrate)
CC {ECO:0000269|PubMed:10714990};
CC KM=0.13 mM for H(2) (methyl viologen as cosubstrate)
CC {ECO:0000269|PubMed:10714990};
CC KM=63 uM for NADPH (H(+) as cosubstrate)
CC {ECO:0000269|PubMed:10714990};
CC KM=71 uM for NADH (H(+) as cosubstrate)
CC {ECO:0000269|PubMed:10714990};
CC KM=17 uM for NADP (H(2) as cosubstrate)
CC {ECO:0000269|PubMed:10714990};
CC KM=125 uM for NAD (H(2) as cosubstrate)
CC {ECO:0000269|PubMed:10714990};
CC KM=0.2 mM for sulfur (H(2) as cosubstrate)
CC {ECO:0000269|PubMed:10714990};
CC KM=0.67 mM for polysulfide (NADPH as cosubstrate)
CC {ECO:0000269|PubMed:10714990};
CC Note=Measured for the whole complex. {ECO:0000269|PubMed:10714990};
CC pH dependence:
CC Optimum pH is 8 for hydrogenase activity at >95 degrees Celsius.
CC {ECO:0000269|PubMed:10714990};
CC Temperature dependence:
CC Optimum temperature is greater than 90 degrees Celsius. Activity
CC increases with increasing temperature from 30 degrees Celsius to 90
CC degrees Celsius. Has a half-life of 6 hours at 95 degrees Celsius.
CC {ECO:0000269|PubMed:10714990};
CC -!- SUBUNIT: Dimer of heterotetramer of alpha, beta, gamma and delta
CC subunits. The nickel-containing alpha and delta subunits constitute the
CC hydrogenase activity. The beta and gamma subunits (flavin-containing
CC dimer) constitute the sulfur reductase activity.
CC {ECO:0000269|PubMed:10714990, ECO:0000269|PubMed:11265463}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10714990}.
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit
CC family. {ECO:0000255}.
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DR EMBL; AF176650; AAF61854.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81456.1; -; Genomic_DNA.
DR RefSeq; WP_011012478.1; NC_018092.1.
DR AlphaFoldDB; E7FHC4; -.
DR SMR; E7FHC4; -.
DR STRING; 186497.PF1332; -.
DR PRIDE; E7FHC4; -.
DR EnsemblBacteria; AAL81456; AAL81456; PF1332.
DR GeneID; 41713135; -.
DR KEGG; pfu:PF1332; -.
DR PATRIC; fig|186497.12.peg.1395; -.
DR eggNOG; arCOG01549; Archaea.
DR HOGENOM; CLU_044556_0_0_2; -.
DR OMA; RICAICY; -.
DR OrthoDB; 32760at2157; -.
DR PhylomeDB; E7FHC4; -.
DR BioCyc; MetaCyc:MON-17852; -.
DR BRENDA; 1.12.1.5; 5243.
DR BRENDA; 1.12.98.4; 5243.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0050583; F:hydrogen dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0047985; F:hydrogen dehydrogenase activity; IEA:RHEA.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR Gene3D; 1.10.645.10; -; 1.
DR InterPro; IPR001501; Ni-dep_hyd_lsu.
DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS.
DR InterPro; IPR029014; NiFe-Hase_large.
DR Pfam; PF00374; NiFeSe_Hases; 2.
DR SUPFAM; SSF56762; SSF56762; 1.
DR PROSITE; PS00508; NI_HGENASE_L_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Iron; Metal-binding; NAD; NADP;
KW Nickel; Oxidoreductase; Reference proteome.
FT CHAIN 1..412
FT /note="Sulfhydrogenase 2 subunit alpha"
FT /id="PRO_0000420725"
FT BINDING 60
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250|UniProtKB:P21852"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P21852"
FT BINDING 63
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250|UniProtKB:P21852"
FT BINDING 402
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250|UniProtKB:P21852"
FT BINDING 405
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P21852"
FT BINDING 405
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000250|UniProtKB:P21852"
SQ SEQUENCE 412 AA; 46180 MW; AB60BBA9906E2658 CRC64;
MIIELDEFTR VEGNGKAEIV IENGEVKDAR VKIVEGPRFF EILTLGRDYW DVPDLEARIC
AICYIAHSVA SVRAIEKALG IDVPESVEKL RELALWGEII ESHALHLYLL ALPDVFGYPD
AISMIPRHGE LVKEGLTIKA FGNAIRELIG GREIHGINIK PGGFGRYPSE EELEKIAEHS
KSLIKFARRI VGIFASQEAG GAVGEVLMAT SDYLWGDELI INGERVQYYE VDEVPVGYSF
AKHSYYKGNP VFVGALPRLL LKGESIEGEA ARMLEEYRDK LESKYVIYNN LAQAIELLYA
LERVPQLVEE ILSEGIERGN GEISQESGEG VGYVEAPRGV LVHHYRIENG KVVWSNTITP
TAFNQRLMEL SLLEEAKRLY GSESEENMKK RLEVIVRAFD PCISCSVHFV KL
