NSR_THEKO
ID NSR_THEKO Reviewed; 442 AA.
AC Q5JGP4;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=NAD(P)H sulfur oxidoreductase (CoA-dependent) {ECO:0000305};
DE Short=NSR {ECO:0000303|PubMed:24723088};
DE EC=1.8.1.18 {ECO:0000269|PubMed:24723088};
DE AltName: Full=NAD(P)H oxidase (H2O-forming) {ECO:0000305};
DE Short=NOX {ECO:0000303|PubMed:24723088};
DE EC=1.6.3.2 {ECO:0000269|PubMed:23453203};
GN OrderedLocusNames=TK1299;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP FUNCTION AS A NAD(P)H OXIDASE, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=23453203; DOI=10.1016/j.jbiosc.2013.01.020;
RA Nisar M.A., Rashid N., Bashir Q., Gardner Q.T., Shafiq M.H., Akhtar M.;
RT "TK1299, a highly thermostable NAD(P)H oxidase from Thermococcus
RT kodakaraensis exhibiting higher enzymatic activity with NADPH.";
RL J. Biosci. Bioeng. 116:39-44(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=24723088; DOI=10.1007/s00792-014-0643-z;
RA Harnvoravongchai P., Kobori H., Orita I., Nakamura S., Imanaka T.,
RA Fukui T.;
RT "Characterization and gene deletion analysis of four homologues of group 3
RT pyridine nucleotide disulfide oxidoreductases from Thermococcus
RT kodakarensis.";
RL Extremophiles 18:603-616(2014).
CC -!- FUNCTION: Catalyzes the CoA-dependent reduction of elemental sulfur
CC (S(0)) to produce hydrogen sulfide. Can use both NADPH and NADH, but
CC shows a preference for NADPH (PubMed:24723088). CoA-SH may act to
CC solubilize S(0) by forming CoA persulfides, followed by the reduction
CC of an enzyme-S-S-CoA intermediate produced after both enzymatic and
CC nonenzymatic evolution of H(2)S from the CoA persulfide
CC (PubMed:24723088). Also catalyzes the oxidation of NADPH as well as
CC NADH and predominantly converts O(2) to H(2)O, with a preference for
CC NADPH (PubMed:23453203). {ECO:0000269|PubMed:23453203,
CC ECO:0000269|PubMed:24723088}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + NADP(+) = NADPH + sulfur;
CC Xref=Rhea:RHEA:36595, ChEBI:CHEBI:26833, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.18;
CC Evidence={ECO:0000269|PubMed:24723088};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:36597;
CC Evidence={ECO:0000269|PubMed:24723088};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + NAD(+) = NADH + sulfur;
CC Xref=Rhea:RHEA:36599, ChEBI:CHEBI:26833, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.18;
CC Evidence={ECO:0000269|PubMed:24723088};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:36601;
CC Evidence={ECO:0000269|PubMed:24723088};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 NADPH + O2 = 2 H2O + 2 NADP(+);
CC Xref=Rhea:RHEA:37795, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.2;
CC Evidence={ECO:0000269|PubMed:23453203};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 NADH + O2 = 2 H2O + 2 NAD(+); Xref=Rhea:RHEA:37799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.2;
CC Evidence={ECO:0000269|PubMed:23453203};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:23453203, ECO:0000269|PubMed:24723088};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O58308};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24 uM for NADH {ECO:0000269|PubMed:23453203};
CC KM=25 uM for NADPH {ECO:0000269|PubMed:23453203};
CC KM=260 uM for CoA-SH {ECO:0000269|PubMed:24723088};
CC Vmax=83 umol/min/mg enzyme for NADH oxidase activity
CC {ECO:0000269|PubMed:23453203};
CC Vmax=61 umol/min/mg enzyme for NADPH oxidase activity
CC {ECO:0000269|PubMed:23453203};
CC Note=kcat is 68 sec(-1) for NADH oxidase activity. kcat is 50 sec(-1)
CC for NADPH oxidase activity. {ECO:0000269|PubMed:23453203};
CC pH dependence:
CC Optimum pH is 8.0 for NAD(P)H oxidase activity.
CC {ECO:0000269|PubMed:23453203};
CC Temperature dependence:
CC Highly thermostable. {ECO:0000269|PubMed:23453203};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:23453203,
CC ECO:0000269|PubMed:24723088}.
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AP006878; BAD85488.1; -; Genomic_DNA.
DR RefSeq; WP_011250250.1; NC_006624.1.
DR AlphaFoldDB; Q5JGP4; -.
DR SMR; Q5JGP4; -.
DR IntAct; Q5JGP4; 1.
DR MINT; Q5JGP4; -.
DR STRING; 69014.TK1299; -.
DR EnsemblBacteria; BAD85488; BAD85488; TK1299.
DR GeneID; 3235301; -.
DR KEGG; tko:TK1299; -.
DR PATRIC; fig|69014.16.peg.1271; -.
DR eggNOG; arCOG01069; Archaea.
DR HOGENOM; CLU_003291_1_3_2; -.
DR InParanoid; Q5JGP4; -.
DR OMA; WVSHAPC; -.
DR OrthoDB; 40511at2157; -.
DR PhylomeDB; Q5JGP4; -.
DR BRENDA; 1.6.3.1; 5246.
DR BRENDA; 1.6.3.2; 5246.
DR BRENDA; 1.8.1.18; 5246.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0050451; F:CoA-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0043914; F:NADPH:sulfur oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 3.
DR InterPro; IPR017758; CoA_disulphide_reductase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR03385; CoA_CoA_reduc; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; NAD; NADP; Oxidoreductase; Redox-active center;
KW Reference proteome.
FT CHAIN 1..442
FT /note="NAD(P)H sulfur oxidoreductase (CoA-dependent)"
FT /id="PRO_0000184700"
FT ACT_SITE 45
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 13..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 24
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 35..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 41..45
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 42..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 62..63
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 72
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 302
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 358
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 422
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 430
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 438
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
SQ SEQUENCE 442 AA; 48610 MW; A51CC778EA62E476 CRC64;
MERKTVVVIG GGAAGMSTAS RVKRLKPEWD VKVFEATEWV SHAPCGIPYV VEGISPKEKL
MHYPPEVFIK KRGIDLHLKA EVIEVEQGRV RVREEDGEKT YEWDYLVFAN GASPQVPAIE
GIDLPGVFTA DLPPDAVAIT EYLEKNPVEN VVVIGTGYIA IEMAEAFVER GKNVTLIGRS
ERVLRKTFDK EITDIVEEKL RNHLNLRLEE VTLRIEGKER VERVVTDAGE YPADLVIVAT
GIKPNTELAR GLGVRIGETG AIWTNDRMQT SVENVYAAGD VAETKHLITG RRVWMPLAPA
GNKMGYVAGS NIAGKEIHFP GVLGTSITKF LDLEIGKTGL TEAEAMKEGY DVRTAFIKAG
TRPHYYPGSK TIWLKGVVDN ETNRLLGVQA VGGDILPRID TAAAMITAGF TTKDVFFTDL
AYAPPFAPVW DPLIVLARVL KF
