SUDHB_PYRFU
ID SUDHB_PYRFU Reviewed; 278 AA.
AC Q8U194; Q9UWJ3;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Sulfide dehydrogenase subunit beta {ECO:0000303|PubMed:7961401};
DE Short=SuDH {ECO:0000303|PubMed:7961401};
DE EC=1.8.1.19 {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
DE AltName: Full=Ferredoxin:NADP oxidoreductase {ECO:0000303|Ref.4};
DE Short=FNOR {ECO:0000303|Ref.4};
DE EC=1.18.1.2 {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
DE Flags: Precursor;
GN Name=sudB {ECO:0000303|PubMed:10968624}; OrderedLocusNames=PF1327;
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]
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 [2]
RP PROTEIN SEQUENCE OF 5-24, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 {ECO:0000269|PubMed:7961401};
RX PubMed=7961401; DOI=10.1128/jb.176.21.6509-6517.1994;
RA Ma K., Adams M.W.;
RT "Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus
RT furiosus: a new multifunctional enzyme involved in the reduction of
RT elemental sulfur.";
RL J. Bacteriol. 176:6509-6517(1994).
RN [3]
RP FUNCTION, COFACTOR, AND EPR SPECTROSCOPY.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000269|PubMed:10968624};
RX PubMed=10968624; DOI=10.1007/pl00021452;
RA Hagen W.R., Silva P.J., Amorim M.A., Hagedoorn P.L., Wassink H., Haaker H.,
RA Robb F.T.;
RT "Novel structure and redox chemistry of the prosthetic groups of the iron-
RT sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus;
RT evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands.";
RL J. Biol. Inorg. Chem. 5:527-534(2000).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 {ECO:0000269|Ref.4};
RX DOI=10.1016/S0076-6879(01)34456-7;
RA Ma K., Adams M.W.;
RT "Ferredoxin:NADP oxidoreductase from Pyrococcus furiosus.";
RL Methods Enzymol. 334:40-45(2001).
CC -!- FUNCTION: A bifunctional enzyme that catalyzes the reduction of
CC elemental sulfur or polysulfide to hydrogen sulfide with NADPH as
CC electron donor. Also functions as a reduced ferredoxin:NADP
CC oxidoreductase with a very high affinity for reduced ferredoxin.
CC Exhibits a broad specificity for various physiological and non-
CC physiological substrates with varied reduction potentials such as
CC methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-
CC dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with
CC highest preference for benzyl viologen. Does not reduce fumarate,
CC succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not
CC possess any hydrogenase activity or NADPH-dependent glutamate synthase
CC activity. {ECO:0000269|PubMed:10968624, ECO:0000269|PubMed:7961401,
CC ECO:0000269|Ref.4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + NADP(+) + n sulfur = NADPH + (n+1) sulfur;
CC Xref=Rhea:RHEA:38451, ChEBI:CHEBI:26833, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.19;
CC Evidence={ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.18.1.2; Evidence={ECO:0000269|PubMed:7961401,
CC ECO:0000269|Ref.4};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10968624, ECO:0000269|PubMed:7961401};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10968624,
CC ECO:0000269|PubMed:7961401};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:10968624, ECO:0000269|PubMed:7961401};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:10968624,
CC ECO:0000269|PubMed:7961401};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for NADPH (with benzyl viologen as cosubstrate at pH 9.5)
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC KM=71 uM for NADH (with benzyl viologen as cosubstrate at pH 9.5)
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC KM=1.25 mM for polysulfide (with NADPH as cosubstrate at pH 8.0)
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC KM=125 uM for benzyl viologen (with NADPH as cosubstrate at pH 9.5)
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC KM=0.7 uM for reduced ferredoxin (with NADP as cosubstrate at pH 8.0)
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC KM=1.6 uM for rubredoxin (with NADPH as cosubstrate at pH 8.0)
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC KM=240 uM for oxygen (with NADPH as cosubstrate at pH 10.2)
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC KM=11 uM for NADPH (with benzyl viologen as cosubstrate at 80 degrees
CC Celsius) {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC KM=71 uM for NADH (with benzyl viologen as cosubstrate at 80 degrees
CC Celsius) {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC KM=1.25 mM for polysulfide (with NADPH as cosubstrate at 80 degrees
CC Celsius) {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC KM=125 uM for benzyl viologen (with NADPH as cosubstrate at 80
CC degrees Celsius) {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC KM=1.6 uM for rubredoxin (with NADPH as cosubstrate at 80 degrees
CC Celsius) {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC KM=240 uM for oxygen (with NADPH as cosubstrate at 80 degrees
CC Celsius) {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC KM=0.7 uM for reduced ferredoxin (with NADP as cosubstrate at 80
CC degrees Celsius) {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC Vmax=263 umol/min/mg enzyme with NADPH as substrate
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC Vmax=182 umol/min/mg enzyme with NADH as substrate
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC Vmax=14 umol/min/mg enzyme with polysulfide as substrate
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC Vmax=278 umol/min/mg enzyme with benzyl viologen as substrate
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC Vmax=8 umol/min/mg enzyme with reduced ferredoxin as substrate
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC Vmax=1 umol/min/mg enzyme with rubredoxin as substrate
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC Vmax=166 umol/min/mg enzyme with oxygen as substrate
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4};
CC Note=Measured for the whole complex. {ECO:0000269|PubMed:7961401};
CC pH dependence:
CC Optimum pH is 8.0 (for polysulfide as substrate) and 10.3 (for benzyl
CC viologen as substrate). {ECO:0000269|PubMed:7961401,
CC ECO:0000269|Ref.4};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius. Has a half-life of 12 h at
CC 95 degrees Celsius. Activity increases by 50% after incubation for
CC several hours at 82 degrees Celsius. {ECO:0000269|PubMed:7961401,
CC ECO:0000269|Ref.4};
CC -!- SUBUNIT: Heterodimer of alpha and beta subunits.
CC {ECO:0000269|PubMed:7961401, ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7961401}.
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DR EMBL; AE009950; AAL81452.1; -; Genomic_DNA.
DR RefSeq; WP_011012474.1; NC_003413.1.
DR PDB; 5JCA; X-ray; 1.50 A; S=1-278.
DR PDB; 5JFC; X-ray; 1.60 A; S=1-278.
DR PDBsum; 5JCA; -.
DR PDBsum; 5JFC; -.
DR AlphaFoldDB; Q8U194; -.
DR SMR; Q8U194; -.
DR STRING; 186497.PF1328; -.
DR PRIDE; Q8U194; -.
DR EnsemblBacteria; AAL81452; AAL81452; PF1328.
DR GeneID; 1469203; -.
DR KEGG; pfu:PF1328; -.
DR PATRIC; fig|186497.12.peg.1391; -.
DR eggNOG; arCOG02199; Archaea.
DR HOGENOM; CLU_003827_1_0_2; -.
DR OMA; AGQFIIL; -.
DR OrthoDB; 50646at2157; -.
DR PhylomeDB; Q8U194; -.
DR BRENDA; 1.6.1.4; 5243.
DR BRENDA; 1.8.1.19; 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:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
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:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF10418; DHODB_Fe-S_bind; 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; 3D-structure; Cytoplasm; Direct protein sequencing; FAD;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome.
FT PROPEP 1..4
FT /evidence="ECO:0000269|PubMed:7961401"
FT /id="PRO_0000420431"
FT CHAIN 5..278
FT /note="Sulfide dehydrogenase subunit beta"
FT /evidence="ECO:0000269|PubMed:7961401"
FT /id="PRO_0000420432"
FT DOMAIN 1..95
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 222
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 225
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT BINDING 237
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:5JCA"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:5JCA"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:5JCA"
SQ SEQUENCE 278 AA; 30817 MW; 82CF5F9135C092A5 CRC64;
MFKILRKERL APGINLFEIE SPRIAKHAKP GQFVMIRLHE KGERIPLTIA DVDISKGSIT
IVAQEVGKTT RELGTYEAGD YILDVLGPLG KPSHIDYFGT VVMIGGGVGV AEIYPVAKAM
KEKGNYVISI LGFRTKDLVF WEDKLRSVSD EVIVTTNDGS YGMKGFTTHA LQKLIEEGRK
IDLVHAVGPA IMMKAVAELT KPYGIKTVAS LNPIMVDGTG MCGACRVTVG GEVKFACVDG
PEFDAHLVDW DQLMNRLAYY RDLEKISLEK WERERRMV
