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Protein

Phosphoadenosine phosphosulfate reductase

Gene

cysH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reduction of activated sulfate into sulfite.

Catalytic activityi

Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin.

Pathwayi: hydrogen sulfide biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes sulfite from sulfate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Sulfate adenylyltransferase subunit 1 (cysN), Sulfate adenylyltransferase subunit 2 (cysD)
  2. Adenylyl-sulfate kinase (cysC)
  3. Phosphoadenosine phosphosulfate reductase (cysH)
This subpathway is part of the pathway hydrogen sulfide biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sulfite from sulfate, the pathway hydrogen sulfide biosynthesis and in Sulfur metabolism.

GO - Molecular functioni

  • phosphoadenylyl-sulfate reductase (thioredoxin) activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

BioCyciEcoCyc:PAPSSULFOTRANS-MONOMER.
ECOL316407:JW2732-MONOMER.
MetaCyc:PAPSSULFOTRANS-MONOMER.
BRENDAi1.8.4.8. 2026.
UniPathwayiUPA00140; UER00206.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoadenosine phosphosulfate reductase (EC:1.8.4.8)
Alternative name(s):
3'-phosphoadenylylsulfate reductase
PAPS reductase, thioredoxin dependent
PAPS sulfotransferase
PAdoPS reductase
Gene namesi
Name:cysH
Ordered Locus Names:b2762, JW2732
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10189. cysH.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi209Y → F: Reduction in Vmax. 1 Publication1
Mutagenesisi239C → S: 5-fold reduction in Vmax. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001006302 – 244Phosphoadenosine phosphosulfate reductaseAdd BLAST243

Proteomic databases

PaxDbiP17854.
PRIDEiP17854.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4261451. 22 interactors.
IntActiP17854. 4 interactors.
STRINGi511145.b2762.

Structurei

Secondary structure

1244
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 10Combined sources5
Helixi14 – 28Combined sources15
Helixi33 – 43Combined sources11
Beta strandi46 – 51Combined sources6
Turni56 – 58Combined sources3
Helixi59 – 68Combined sources10
Beta strandi73 – 78Combined sources6
Helixi84 – 96Combined sources13
Beta strandi100 – 105Combined sources6
Helixi110 – 117Combined sources8
Helixi120 – 122Combined sources3
Helixi124 – 135Combined sources12
Helixi137 – 146Combined sources10
Beta strandi149 – 153Combined sources5
Beta strandi160 – 162Combined sources3
Turni163 – 166Combined sources4
Beta strandi169 – 173Combined sources5
Beta strandi176 – 179Combined sources4
Turni181 – 184Combined sources4
Helixi187 – 197Combined sources11
Helixi203 – 207Combined sources5
Turni216 – 218Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SURX-ray2.00A2-216[»]
2O8VX-ray3.00A1-244[»]
ProteinModelPortaliP17854.
SMRiP17854.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17854.

Family & Domainsi

Sequence similaritiesi

Belongs to the PAPS reductase family. CysH subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105ET3. Bacteria.
COG0175. LUCA.
HOGENOMiHOG000249396.
InParanoidiP17854.
KOiK00390.
OMAiPRNKLLD.
PhylomeDBiP17854.

Family and domain databases

CDDicd01713. PAPS_reductase. 1 hit.
Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00063. CysH. 1 hit.
InterProiIPR004511. PAPS/APS_Rdtase.
IPR002500. PAPS_reduct.
IPR011800. PAPS_reductase_CysH.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01507. PAPS_reduct. 1 hit.
[Graphical view]
PIRSFiPIRSF000857. PAPS_reductase. 1 hit.
TIGRFAMsiTIGR00434. cysH. 1 hit.
TIGR02057. PAPS_reductase. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P17854-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKLDLNALN ELPKVDRILA LAETNAELEK LDAEGRVAWA LDNLPGEYVL
60 70 80 90 100
SSSFGIQAAV SLHLVNQIRP DIPVILTDTG YLFPETYRFI DELTDKLKLN
110 120 130 140 150
LKVYRATESA AWQEARYGKL WEQGVEGIEK YNDINKVEPM NRALKELNAQ
160 170 180 190 200
TWFAGLRREQ SGSRANLPVL AIQRGVFKVL PIIDWDNRTI YQYLQKHGLK
210 220 230 240
YHPLWDEGYL SVGDTHTTRK WEPGMAEEET RFFGLKRECG LHEG
Length:244
Mass (Da):27,976
Last modified:January 23, 2007 - v3
Checksum:i7EC494ED2437E469
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti27E → Q in AAA23652 (PubMed:2670946).Curated1
Sequence conflicti226A → S in AAA23652 (PubMed:2670946).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07525 Genomic DNA. Translation: CAA68817.1.
M23008 Genomic DNA. Translation: AAA23652.1.
U29579 Genomic DNA. Translation: AAA69272.1.
U00096 Genomic DNA. Translation: AAC75804.1.
AP009048 Genomic DNA. Translation: BAE76839.1.
PIRiS14221. RDECPA.
RefSeqiNP_417242.1. NC_000913.3.
WP_000039850.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75804; AAC75804; b2762.
BAE76839; BAE76839; BAE76839.
GeneIDi947230.
KEGGiecj:JW2732.
eco:b2762.
PATRICi32120936. VBIEscCol129921_2860.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07525 Genomic DNA. Translation: CAA68817.1.
M23008 Genomic DNA. Translation: AAA23652.1.
U29579 Genomic DNA. Translation: AAA69272.1.
U00096 Genomic DNA. Translation: AAC75804.1.
AP009048 Genomic DNA. Translation: BAE76839.1.
PIRiS14221. RDECPA.
RefSeqiNP_417242.1. NC_000913.3.
WP_000039850.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SURX-ray2.00A2-216[»]
2O8VX-ray3.00A1-244[»]
ProteinModelPortaliP17854.
SMRiP17854.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261451. 22 interactors.
IntActiP17854. 4 interactors.
STRINGi511145.b2762.

Proteomic databases

PaxDbiP17854.
PRIDEiP17854.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75804; AAC75804; b2762.
BAE76839; BAE76839; BAE76839.
GeneIDi947230.
KEGGiecj:JW2732.
eco:b2762.
PATRICi32120936. VBIEscCol129921_2860.

Organism-specific databases

EchoBASEiEB0186.
EcoGeneiEG10189. cysH.

Phylogenomic databases

eggNOGiENOG4105ET3. Bacteria.
COG0175. LUCA.
HOGENOMiHOG000249396.
InParanoidiP17854.
KOiK00390.
OMAiPRNKLLD.
PhylomeDBiP17854.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00206.
BioCyciEcoCyc:PAPSSULFOTRANS-MONOMER.
ECOL316407:JW2732-MONOMER.
MetaCyc:PAPSSULFOTRANS-MONOMER.
BRENDAi1.8.4.8. 2026.

Miscellaneous databases

EvolutionaryTraceiP17854.
PROiP17854.

Family and domain databases

CDDicd01713. PAPS_reductase. 1 hit.
Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00063. CysH. 1 hit.
InterProiIPR004511. PAPS/APS_Rdtase.
IPR002500. PAPS_reduct.
IPR011800. PAPS_reductase_CysH.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01507. PAPS_reduct. 1 hit.
[Graphical view]
PIRSFiPIRSF000857. PAPS_reductase. 1 hit.
TIGRFAMsiTIGR00434. cysH. 1 hit.
TIGR02057. PAPS_reductase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCYSH_ECOLI
AccessioniPrimary (citable) accession number: P17854
Secondary accession number(s): Q2MA67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.