HYD1G_PYRFU
ID HYD1G_PYRFU Reviewed; 292 AA.
AC Q8U2E4; Q59668;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Sulfhydrogenase 1 subunit gamma;
DE EC=1.12.98.4;
DE AltName: Full=Sulfhydrogenase I subunit gamma {ECO:0000303|PubMed:7704275};
DE AltName: Full=Sulfur reductase subunit HydG {ECO:0000303|PubMed:7704275};
GN Name=hydG {ECO:0000303|PubMed:7704275}; OrderedLocusNames=PF0892;
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}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 {ECO:0000269|PubMed:7704275};
RX PubMed=7704275; DOI=10.1099/13500872-141-2-449;
RA Pedroni P., Della Volpe A., Galli G., Mura G.M., Pratesi C., Grandi G.;
RT "Characterization of the locus encoding the [Ni-Fe] sulfhydrogenase from
RT the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial
RT sulfite reductases.";
RL Microbiology 141:449-458(1995).
RN [2] {ECO:0000312|EMBL:AAL81016.1}
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, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 {ECO:0000269|PubMed:8389482};
RX PubMed=8389482; DOI=10.1073/pnas.90.11.5341;
RA Ma K., Schicho R.N., Kelly R.M., Adams M.W.;
RT "Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental
RT sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing
RT hydrogenase ancestor.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5341-5344(1993).
RN [4] {ECO:0000305}
RP SUBUNIT, AND EPR SPECTROSCOPY.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 {ECO:0000269|PubMed:7615063};
RX PubMed=7615063; DOI=10.1016/0014-5793(95)00622-g;
RA Arendsen A.F., Veenhuizen P.T., Hagen W.R.;
RT "Redox properties of the sulfhydrogenase from Pyrococcus furiosus.";
RL FEBS Lett. 368:117-121(1995).
RN [5] {ECO:0000305}
RP FUNCTION, COFACTOR, AND EPR SPECTROSCOPY.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000269|PubMed:10439073};
RX PubMed=10439073; DOI=10.1007/s007750050314;
RA Silva P.J., de Castro B., Hagen W.R.;
RT "On the prosthetic groups of the NiFe sulfhydrogenase from Pyrococcus
RT furiosus: topology, structure, and temperature-dependent redox chemistry.";
RL J. Biol. Inorg. Chem. 4:284-291(1999).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 an
CC NADPH-dependent hydrogen-evolving hydrogenase with sulfur reducing
CC activity. May play a role in hydrogen cycling during fermentative
CC growth. Activity not exhibited with NAD. The beta and gamma subunits
CC form the sulfur reducing component that catalyzes the cytoplasmic
CC production of hydrogen sulfide in the presence of elemental sulfur. Not
CC active in the presence of sodium sulfate, sodium sulfite, sodium
CC thiosulfate or cysteine. {ECO:0000269|PubMed:10439073,
CC ECO:0000269|PubMed:11265463, ECO:0000269|PubMed:7704275,
CC ECO:0000269|PubMed:8389482}.
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:11265463, ECO:0000269|PubMed:8389482};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10439073};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10439073};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:10439073};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:10439073};
CC -!- ACTIVITY REGULATION: Stimulated by rubredoxin at pH 7.6 but not
CC ferredoxin. {ECO:0000269|PubMed:8389482}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=6 umol/min/mg enzyme {ECO:0000269|PubMed:11265463,
CC ECO:0000269|PubMed:8389482};
CC Note=Measured for the whole complex. {ECO:0000269|PubMed:11265463};
CC pH dependence:
CC Optimum pH is 8.4 for sulfur reductase activity at 80 degrees
CC Celsius. {ECO:0000269|PubMed:11265463, ECO:0000269|PubMed:8389482};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius for maximal sulfur
CC reductase activity. Activity increases linearly from above 30 degrees
CC Celsius to reach maximal levels at 80 degrees Celsius and then
CC decreases to 15% of activity at 90 degrees Celsius.
CC {ECO:0000269|PubMed:11265463, ECO:0000269|PubMed:8389482};
CC -!- SUBUNIT: Heterotetramer of alpha, beta, gamma and delta subunits. The
CC nickel-containing alpha and delta subunits constitute the hydrogenase
CC activity. The beta and gamma subunits (flavin-containing dimer)
CC constitute the sulfur reductase activity. {ECO:0000269|PubMed:7615063,
CC ECO:0000269|PubMed:7704275, ECO:0000269|PubMed:8389482}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7704275,
CC ECO:0000269|PubMed:8389482}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA53035.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X75255; CAA53035.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE009950; AAL81016.1; -; Genomic_DNA.
DR PIR; S48834; S48834.
DR RefSeq; WP_011012027.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U2E4; -.
DR SMR; Q8U2E4; -.
DR STRING; 186497.PF0892; -.
DR EnsemblBacteria; AAL81016; AAL81016; PF0892.
DR GeneID; 41712700; -.
DR KEGG; pfu:PF0892; -.
DR PATRIC; fig|186497.12.peg.943; -.
DR eggNOG; arCOG02199; Archaea.
DR HOGENOM; CLU_003827_1_1_2; -.
DR OMA; NTARYGK; -.
DR OrthoDB; 67226at2157; -.
DR PhylomeDB; Q8U2E4; -.
DR BioCyc; MetaCyc:MON-16383; -.
DR BRENDA; 1.12.1.3; 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; IPR008333; Cbr1-like_FAD-bd_dom.
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; 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; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
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..292
FT /note="Sulfhydrogenase 1 subunit gamma"
FT /id="PRO_0000420728"
FT DOMAIN 15..115
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 253
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 261
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P56968"
FT BINDING 273
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P56968"
SQ SEQUENCE 292 AA; 33054 MW; 771EBBF4B7DE50FA CRC64;
MMLPKEIMMP NDNPYALHRV KVLKVYSLTE TEKLFLFRFE DPELAEKWTF KPGQFVQLTI
PGVGEVPISI CSSPMRKGFF ELCIRKAGRV TTVVHRLKPG DTVLVRGPYG NGFPVDEWEG
MDLLLIAAGL GTAPLRSVFL YAMDNRWKYG NITFINTARY GKDLLFYKEL EAMKDLAEAE
NVKIIQSVTR DPNWPGLKGR PQQFIVEANT NPKNTAVAIC GPPRMYKSVF EALINYGYRP
ENIFVTLERR MKCGIGKCGH CNVGTSTSWK YICKDGPVFT YFDIVSTPGL LD
