HYD2G_PYRFU
ID HYD2G_PYRFU Reviewed; 288 AA.
AC E7FHW8; Q7LWY8; Q9P9M6;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Sulfhydrogenase 2 subunit gamma;
DE EC=1.12.98.4;
DE AltName: Full=Hydrogenase-II subunit gamma {ECO:0000303|PubMed:10714990};
DE Short=H-II gamma {ECO:0000303|PubMed:10714990};
DE AltName: Full=Sulfhydrogenase II subunit gamma {ECO:0000303|PubMed:10714990};
DE AltName: Full=Sulfur reductase subunit ShyC {ECO:0000303|PubMed:10714990};
GN Name=shyC {ECO:0000312|EMBL:AAF61852.1}; OrderedLocusNames=PF1330;
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:AAF61852.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12, 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:AAF61852.1};
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:AAL81454.1}
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=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10714990};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10714990};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:10714990};
CC Note=Binds 1 [2Fe-2S] cluster. {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; AAF61852.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81454.1; -; Genomic_DNA.
DR RefSeq; WP_011012476.1; NC_018092.1.
DR AlphaFoldDB; E7FHW8; -.
DR SMR; E7FHW8; -.
DR STRING; 186497.PF1330; -.
DR PRIDE; E7FHW8; -.
DR EnsemblBacteria; AAL81454; AAL81454; PF1330.
DR GeneID; 41713133; -.
DR KEGG; pfu:PF1330; -.
DR PATRIC; fig|186497.12.peg.1393; -.
DR eggNOG; arCOG02199; Archaea.
DR HOGENOM; CLU_003827_1_1_2; -.
DR OMA; YMTLERR; -.
DR OrthoDB; 67226at2157; -.
DR PhylomeDB; E7FHW8; -.
DR BioCyc; MetaCyc:MON-17851; -.
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:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033796; F:sulfur reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR Gene3D; 2.10.240.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR InterPro; IPR037117; Dihydroorotate_DH_ele_sf.
DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Direct protein sequencing; Electron transport; FAD;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome; Transport.
FT CHAIN 1..288
FT /note="Sulfhydrogenase 2 subunit gamma"
FT /id="PRO_0000420729"
FT DOMAIN 4..103
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 250
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P56968"
FT BINDING 255
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P56968"
FT BINDING 258
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P56968"
FT BINDING 270
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P56968"
SQ SEQUENCE 288 AA; 32945 MW; 4760C3B6CE8B1840 CRC64;
MNPYRSYDAR IIEVKELTSR EKLFSLKFLD NEIEENFTFK PGQFVIVDIR GFGEFPISLC
SSPTRRPIQL CIRRVGRMTK FIHKMNEGDI IGIRGPYGNG FPMDLMEGSN LILIAGGLGM
APLRSVLWYA IDSGKYEKIY LFYGTKSYED ILFRDEIIHL LKHGEKLNCH VKLAYEVETP
SCIYLERGFS EKVCKGVVTD LFRGEEFDVE NSYALICGPP VMYKYVIREL LDRGLSPGRI
YMTLERRMRC GVGKCGHCIV GTSVSIKYIC KDGPVFTYWD ALSTRGLI
