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Protein

Sulfide dehydrogenase subunit beta

Gene

sudB

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.3 Publications

Catalytic activityi

Hydrogen sulfide + (sulfide)(n) + NADP+ = (sulfide)(n+1) + NADPH.2 Publications
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH.2 Publications

Cofactori

Protein has several cofactor binding sites:
  • FAD2 PublicationsNote: Binds 1 FAD per subunit.2 Publications
  • [2Fe-2S] cluster2 PublicationsNote: Binds 1 [2Fe-2S] cluster.2 Publications

Kineticsi

Measured for the whole complex.1 Publication

  1. KM=11 µM for NADPH (with benzyl viologen as cosubstrate at pH 9.5)2 Publications
  2. KM=71 µM for NADH (with benzyl viologen as cosubstrate at pH 9.5)2 Publications
  3. KM=1.25 mM for polysulfide (with NADPH as cosubstrate at pH 8.0)2 Publications
  4. KM=125 µM for benzyl viologen (with NADPH as cosubstrate at pH 9.5)2 Publications
  5. KM=0.7 µM for reduced ferredoxin (with NADP as cosubstrate at pH 8.0)2 Publications
  6. KM=1.6 µM for rubredoxin (with NADPH as cosubstrate at pH 8.0)2 Publications
  7. KM=240 µM for oxygen (with NADPH as cosubstrate at pH 10.2)2 Publications
  8. KM=11 µM for NADPH (with benzyl viologen as cosubstrate at 80 degrees Celsius)2 Publications
  9. KM=71 µM for NADH (with benzyl viologen as cosubstrate at 80 degrees Celsius)2 Publications
  10. KM=1.25 mM for polysulfide (with NADPH as cosubstrate at 80 degrees Celsius)2 Publications
  11. KM=125 µM for benzyl viologen (with NADPH as cosubstrate at 80 degrees Celsius)2 Publications
  12. KM=1.6 µM for rubredoxin (with NADPH as cosubstrate at 80 degrees Celsius)2 Publications
  13. KM=240 µM for oxygen (with NADPH as cosubstrate at 80 degrees Celsius)2 Publications
  14. KM=0.7 µM for reduced ferredoxin (with NADP as cosubstrate at 80 degrees Celsius)2 Publications
  1. Vmax=263 µmol/min/mg enzyme with NADPH as substrate2 Publications
  2. Vmax=182 µmol/min/mg enzyme with NADH as substrate2 Publications
  3. Vmax=14 µmol/min/mg enzyme with polysulfide as substrate2 Publications
  4. Vmax=278 µmol/min/mg enzyme with benzyl viologen as substrate2 Publications
  5. Vmax=8 µmol/min/mg enzyme with reduced ferredoxin as substrate2 Publications
  6. Vmax=1 µmol/min/mg enzyme with rubredoxin as substrate2 Publications
  7. Vmax=166 µmol/min/mg enzyme with oxygen as substrate2 Publications

pH dependencei

Optimum pH is 8.0 (for polysulfide as substrate) and 10.3 (for benzyl viologen as substrate).2 Publications

Temperature dependencei

Optimum temperature is 80 degrees Celsius. Has a half-life of 12 h at 95 degrees Celsius. Activity increases by 50% after incubation for several hours at 82 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi222 – 2221Iron-sulfur (2Fe-2S)Sequence analysis
Metal bindingi225 – 2251Iron-sulfur (2Fe-2S)Sequence analysis
Metal bindingi237 – 2371Iron-sulfur (2Fe-2S)Sequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, NADP

Enzyme and pathway databases

BRENDAi1.8.1.19. 5243.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfide dehydrogenase subunit beta1 Publication (EC:1.8.1.192 Publications)
Short name:
SuDH1 Publication
Alternative name(s):
Ferredoxin:NADP oxidoreductase1 Publication (EC:1.18.1.22 Publications)
Short name:
FNOR1 Publication
Gene namesi
Name:sudB1 Publication
Ordered Locus Names:PF1327
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000001013 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 441 PublicationPRO_0000420431
Chaini5 – 278274Sulfide dehydrogenase subunit beta1 PublicationPRO_0000420432Add
BLAST

Proteomic databases

PRIDEiQ8U194.

Interactioni

Subunit structurei

Heterodimer of alpha and beta subunits.2 Publications

Protein-protein interaction databases

STRINGi186497.PF1328.

Structurei

3D structure databases

ProteinModelPortaliQ8U194.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9595FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiarCOG02199. Archaea.
COG0543. LUCA.
HOGENOMiHOG000225117.
KOiK20203.
OMAiGPIPMMK.

Family and domain databases

InterProiIPR012165. Cyt_c3_hydrogenase_gsu.
IPR019480. Dihydroorotate_DH_Fe-S-bd.
IPR017927. Fd_Rdtase_FAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF10418. DHODB_Fe-S_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF006816. Cyc3_hyd_g. 1 hit.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8U194-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKILRKERL APGINLFEIE SPRIAKHAKP GQFVMIRLHE KGERIPLTIA
60 70 80 90 100
DVDISKGSIT IVAQEVGKTT RELGTYEAGD YILDVLGPLG KPSHIDYFGT
110 120 130 140 150
VVMIGGGVGV AEIYPVAKAM KEKGNYVISI LGFRTKDLVF WEDKLRSVSD
160 170 180 190 200
EVIVTTNDGS YGMKGFTTHA LQKLIEEGRK IDLVHAVGPA IMMKAVAELT
210 220 230 240 250
KPYGIKTVAS LNPIMVDGTG MCGACRVTVG GEVKFACVDG PEFDAHLVDW
260 270
DQLMNRLAYY RDLEKISLEK WERERRMV
Length:278
Mass (Da):30,817
Last modified:June 1, 2002 - v1
Checksum:i82CF5F9135C092A5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL81452.1.
RefSeqiWP_011012474.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL81452; AAL81452; PF1328.
GeneIDi1469203.
KEGGipfu:PF1328.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL81452.1.
RefSeqiWP_011012474.1. NC_003413.1.

3D structure databases

ProteinModelPortaliQ8U194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF1328.

Proteomic databases

PRIDEiQ8U194.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL81452; AAL81452; PF1328.
GeneIDi1469203.
KEGGipfu:PF1328.

Phylogenomic databases

eggNOGiarCOG02199. Archaea.
COG0543. LUCA.
HOGENOMiHOG000225117.
KOiK20203.
OMAiGPIPMMK.

Enzyme and pathway databases

BRENDAi1.8.1.19. 5243.

Family and domain databases

InterProiIPR012165. Cyt_c3_hydrogenase_gsu.
IPR019480. Dihydroorotate_DH_Fe-S-bd.
IPR017927. Fd_Rdtase_FAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF10418. DHODB_Fe-S_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF006816. Cyc3_hyd_g. 1 hit.
SUPFAMiSSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSUDHB_PYRFU
AccessioniPrimary (citable) accession number: Q8U194
Secondary accession number(s): Q9UWJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: June 1, 2002
Last modified: July 6, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.