SUDHA_PYRFU
ID SUDHA_PYRFU Reviewed; 474 AA.
AC Q8U195; Q9UWJ4;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Sulfide dehydrogenase subunit alpha {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=sudA {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 3-18, 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=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000269|PubMed:10968624, ECO:0000269|PubMed:7961401};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000269|PubMed:10968624,
CC ECO:0000269|PubMed:7961401};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:10968624, ECO:0000269|PubMed:7961401};
CC Note=Binds 1 [4Fe-4S] 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; AAL81451.1; -; Genomic_DNA.
DR RefSeq; WP_011012473.1; NZ_CP023154.1.
DR PDB; 5JCA; X-ray; 1.50 A; L=1-474.
DR PDB; 5JFC; X-ray; 1.60 A; L=1-474.
DR PDBsum; 5JCA; -.
DR PDBsum; 5JFC; -.
DR AlphaFoldDB; Q8U195; -.
DR SMR; Q8U195; -.
DR STRING; 186497.PF1327; -.
DR PRIDE; Q8U195; -.
DR EnsemblBacteria; AAL81451; AAL81451; PF1327.
DR GeneID; 41713130; -.
DR KEGG; pfu:PF1327; -.
DR PATRIC; fig|186497.12.peg.1390; -.
DR eggNOG; arCOG01292; Archaea.
DR HOGENOM; CLU_000422_3_3_2; -.
DR OMA; QETQCEQ; -.
DR OrthoDB; 83293at2157; -.
DR PhylomeDB; Q8U195; -.
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:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR006004; Glut_synth_NADPH.
DR InterPro; IPR009051; Helical_ferredxn.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR TIGRFAMs; TIGR01316; gltA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 3Fe-4S; 4Fe-4S; Cytoplasm; Direct protein sequencing; FAD;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome.
FT PROPEP 1..2
FT /evidence="ECO:0000269|PubMed:7961401"
FT /id="PRO_0000420429"
FT CHAIN 3..474
FT /note="Sulfide dehydrogenase subunit alpha"
FT /evidence="ECO:0000269|PubMed:7961401"
FT /id="PRO_0000420430"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 101
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000255"
FT BINDING 107
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000255"
FT BINDING 111
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000255"
FT CONFLICT 18
FT /note="E -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:5JCA"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:5JCA"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:5JCA"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5JCA"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:5JCA"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 268..276
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:5JCA"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 303..314
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 334..343
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 350..358
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 362..377
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 381..395
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 397..401
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 409..414
FT /evidence="ECO:0007829|PDB:5JCA"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:5JCA"
FT HELIX 452..471
FT /evidence="ECO:0007829|PDB:5JCA"
SQ SEQUENCE 474 AA; 52729 MW; 9A6198392CD36585 CRC64;
MPRLIKDRVP TPERSVGERV RDFGEVNLGY SWELALREAE RCLQCPVEYA PCIKGCPVHI
NIPGFIKALR ENRDNPSKAV REALRIIWRD NTLPAITGRV CPQEEQCEGA CVVGKVGDPI
NIGKLERFVA DYAREHGIDD ELLLEEIKGI KRNGKKVAII GAGPAGLTCA ADLAKMGYEV
TIYEALHQPG GVLIYGIPEF RLPKEIVKKE LENLRRLGVK IETNVLVGKT ITFEELREEY
DAIFIGTGAG TPRIYPWPGV NLNGIYSANE FLTRINLMKA YKFPEYDTPI KVGKRVAVIG
GGNTAMDAAR SALRLGAEVW ILYRRTRKEM TAREEEIKHA EEEGVKFMFL VTPKRFIGDE
NGNLKAIELE KMKLGEPDES GRRRPIPTGE TFIMEFDTAI IAIGQTPNKT FLETVPGLKV
DEWGRIVVDE NLMTSIPGVF AGGDAIRGEA TVILAMGDGR KAAKAIHQYL SKEK
