HYD2B_PYRFU
ID HYD2B_PYRFU Reviewed; 334 AA.
AC E7FHN9; Q7LWY9; Q9P9M7;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Sulfhydrogenase 2 subunit beta;
DE EC=1.12.98.4;
DE AltName: Full=Hydrogenase-II subunit beta {ECO:0000303|PubMed:10714990};
DE Short=H-II beta {ECO:0000303|PubMed:10714990};
DE AltName: Full=Sulfhydrogenase II subunit beta {ECO:0000303|PubMed:10714990};
DE AltName: Full=Sulfur reductase subunit ShyB {ECO:0000303|PubMed:10714990};
GN Name=shyB {ECO:0000312|EMBL:AAF61851.1}; OrderedLocusNames=PF1329;
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:AAF61851.1}
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:AAF61851.1};
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:AAL81453.1}
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 beta and gamma subunits form the
CC sulfur-reducing component that catalyzes the cytoplasmic production of
CC hydrogen sulfide in the presence of elemental sulfur.
CC {ECO:0000269|PubMed:10714990, ECO:0000269|PubMed:11133967,
CC ECO:0000269|PubMed:11265463}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2 + n sulfur = H(+) + hydrogen sulfide + (n-1) sulfur;
CC Xref=Rhea:RHEA:35591, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276,
CC ChEBI:CHEBI:26833, ChEBI:CHEBI:29919; EC=1.12.98.4;
CC Evidence={ECO:0000269|PubMed:10714990, ECO:0000269|PubMed:11265463};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:10714990};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000269|PubMed:10714990};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
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 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}.
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DR EMBL; AF176650; AAF61851.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81453.1; -; Genomic_DNA.
DR RefSeq; WP_011012475.1; NC_018092.1.
DR AlphaFoldDB; E7FHN9; -.
DR STRING; 186497.PF1329; -.
DR PRIDE; E7FHN9; -.
DR DNASU; 1469204; -.
DR EnsemblBacteria; AAL81453; AAL81453; PF1329.
DR GeneID; 41713132; -.
DR KEGG; pfu:PF1329; -.
DR PATRIC; fig|186497.12.peg.1392; -.
DR eggNOG; arCOG05128; Archaea.
DR HOGENOM; CLU_046702_0_0_2; -.
DR OMA; DEYCFCK; -.
DR OrthoDB; 34322at2157; -.
DR PhylomeDB; E7FHN9; -.
DR BioCyc; MetaCyc:MON-12580; -.
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:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033796; F:sulfur reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1060.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009051; Helical_ferredxn.
DR Pfam; PF17179; Fer4_22; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Reference proteome; Repeat.
FT CHAIN 1..334
FT /note="Sulfhydrogenase 2 subunit beta"
FT /id="PRO_0000420727"
FT DOMAIN 220..250
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 294..328
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 229
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00198"
FT BINDING 232
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00198"
FT BINDING 235
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00198"
FT BINDING 239
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00198"
FT BINDING 306
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00198"
FT BINDING 309
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00198"
FT BINDING 312
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00198"
FT BINDING 316
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00198"
SQ SEQUENCE 334 AA; 39181 MW; 1A0D9AA471F5AC06 CRC64;
MRYVKLHSEY FPEFFNRLKE VGRVYGPVRH NSTYRFEEVN SIDELSLDYT RTILPPKKFF
IRPRDAMFKI QKNEVTEVDG DGKFVLFGVH SCDIHGIKIL DKVYLSNPPD PYYERRRKNA
FIVGISCMPD EYCFCKSLGT DFAMDGFDIF LHELPDGWLV RVGSVKGHEF VWENQDIFDD
VTEEDLRNFK EFEEKRAKAF KKSLNKEGLA DILDLAFTSK VWKKYAEKCL GCGNCTIVCP
TCRCYEVCDT WVRAYEALRM RRYDSCFMPT HGLVAGGHNF RPTRLDRFRH RYYCKNYFDP
EAGFNCVGCG RCDEFCPARI EHVKVLDEVR EGLI
