NSR_PYRAB
ID NSR_PYRAB Reviewed; 446 AA.
AC Q9UYU5; G8ZHL9;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=NAD(P)H sulfur oxidoreductase (CoA-dependent) {ECO:0000250|UniProtKB:Q8U1M0};
DE Short=NSR {ECO:0000250|UniProtKB:Q8U1M0};
DE EC=1.8.1.18 {ECO:0000250|UniProtKB:Q8U1M0};
GN OrderedLocusNames=PYRAB14120; ORFNames=PAB0936;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- FUNCTION: Catalyzes the CoA-dependent reduction of elemental sulfur
CC (S(0)) to produce hydrogen sulfide. {ECO:0000250|UniProtKB:Q8U1M0}.
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:0000250|UniProtKB:Q8U1M0};
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:0000250|UniProtKB:Q8U1M0};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O58308};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O58308};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AJ248287; CAB50317.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70856.1; -; Genomic_DNA.
DR PIR; H75052; H75052.
DR AlphaFoldDB; Q9UYU5; -.
DR SMR; Q9UYU5; -.
DR STRING; 272844.PAB0936; -.
DR EnsemblBacteria; CAB50317; CAB50317; PAB0936.
DR KEGG; pab:PAB0936; -.
DR PATRIC; fig|272844.11.peg.1501; -.
DR eggNOG; arCOG01069; Archaea.
DR HOGENOM; CLU_003291_1_3_2; -.
DR OMA; WVSHAPC; -.
DR PhylomeDB; Q9UYU5; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 3: Inferred from homology;
KW FAD; Flavoprotein; NAD; NADP; Oxidoreductase; Redox-active center.
FT CHAIN 1..446
FT /note="NAD(P)H sulfur oxidoreductase (CoA-dependent)"
FT /id="PRO_0000184697"
FT ACT_SITE 49
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 17..18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 28
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 39..40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 45..49
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 46..48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 66..67
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 76
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 284
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 306
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 362
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 426
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 434
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
FT BINDING 442
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O58308"
SQ SEQUENCE 446 AA; 49181 MW; 0B7048662F50BD72 CRC64;
MRVVKVKKTV VIIGGGAAGM SAASRVKRLK PEWDVKVFEA TEWVSHAPCG IPYVVEGISP
TEKLMHYPPE VFIKKRGIDL HLNAEVIEVD TGYVRVREKD GEKSYEWDYL VFANGASPQV
PAIEGVDLKG VFTADLPPDA VAIREYMEKN RVEDVVIVGG GYIGLEMAEA FVAQGKRVTM
IVRGERILRR SFDKEVTDII EEKLKQHVNL RLQEIVLRIE GKDRVEKVVT DAGEYRADLV
ILATGIKPNI ELARQLGVRI GETGAIWTNE KMQTSVENVY AAGDVAETKH VITGRRVWVP
LAPPGNKMGY VAGSNIAGKE IHFPGVLGTT VTKFLDVEIG KTGLTETEAL KEGYDIRTAF
IKASTRPHYY PGGKEIWLKG VVDNETNRLL GVQAVGAEIL PRIDAAAAML MANFTTKDAF
FTDLAYAPPF APVWDPLVVL ARVLKF
