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Database: UniProt
Entry: E7FHN9
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Original site: E7FHN9 
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   16-JAN-2019, entry version 39.
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,
RP   SUBCELLULAR 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
RT   archaeon Pyrococcus furiosus and assessment of its role in sulfur
RT   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;
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
RT   P. 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.,
RA   Sapra R., 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
CC       a hydrogen-evolving hydrogenase with sulfur-reducing activity. May
CC       play a role in hydrogen cycling during fermentative growth.
CC       Activity exhibited with NAD in addition to NADPH. The beta and
CC       gamma subunits form the sulfur-reducing component that catalyzes
CC       the cytoplasmic production of hydrogen sulfide in the presence of
CC       elemental sulfur. {ECO:0000269|PubMed:10714990,
CC       ECO:0000269|PubMed:11133967, 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,
CC         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.
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
CC         90 degrees Celsius. Has a half-life of 6 hours at 95 degrees
CC         Celsius. {ECO:0000269|PubMed:10714990};
CC   -!- SUBUNIT: Dimer of heterotetramer of alpha, beta, gamma and delta
CC       subunits. The nickel-containing alpha and delta subunits
CC       constitute the hydrogenase activity. The beta and gamma subunits
CC       (flavin-containing dimer) constitute the sulfur reductase
CC       activity. {ECO:0000269|PubMed:10714990,
CC       ECO:0000269|PubMed:11265463}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10714990}.
DR   EMBL; AF176650; AAF61851.1; -; Genomic_DNA.
DR   EMBL; AE009950; AAL81453.1; -; Genomic_DNA.
DR   RefSeq; WP_011012475.1; NC_003413.1.
DR   ProteinModelPortal; E7FHN9; -.
DR   STRING; 186497.PF1329; -.
DR   PRIDE; E7FHN9; -.
DR   DNASU; 1469204; -.
DR   EnsemblBacteria; AAL81453; AAL81453; PF1329.
DR   GeneID; 1469204; -.
DR   KEGG; pfu:PF1329; -.
DR   PATRIC; fig|186497.12.peg.1392; -.
DR   eggNOG; arCOG05128; Archaea.
DR   eggNOG; COG1145; LUCA.
DR   HOGENOM; HOG000227558; -.
DR   KO; K17996; -.
DR   OMA; DEYCFCK; -.
DR   OrthoDB; 34322at2157; -.
DR   BioCyc; MetaCyc:MONOMER-12580; -.
DR   BioCyc; PFUR186497:G1FZR-1358-MONOMER; -.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   SUPFAM; SSF46548; SSF46548; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Complete proteome; Cytoplasm; Direct protein sequencing; Iron;
KW   Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome;
KW   Repeat.
FT   CHAIN         1    334       Sulfhydrogenase 2 subunit beta.
FT                                /FTId=PRO_0000420727.
FT   DOMAIN      220    250       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      294    328       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       229    229       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00198}.
FT   METAL       232    232       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00198}.
FT   METAL       235    235       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00198}.
FT   METAL       239    239       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00198}.
FT   METAL       306    306       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00198}.
FT   METAL       309    309       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00198}.
FT   METAL       312    312       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000250|UniProtKB:P00198}.
FT   METAL       316    316       Iron-sulfur 2 (4Fe-4S).
FT                                {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
//
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