Phosphoadenosine phosphosulfate reductase - Escherichia coli (strain K12)

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P17854 (CYSH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	cysH
Ordered Locus Names:	b2762, JW2732

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Reduction of activated sulfate into sulfite. HAMAP-Rule MF_00063
Catalytic activity	Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin. HAMAP-Rule MF_00063
Pathway	Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 3/3. HAMAP-Rule MF_00063
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP-Rule MF_00063.
Sequence similarities	Belongs to the PAPS reductase family. CysH subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cysteine biosynthetic process Inferred from electronic annotation. Source: InterPro hydrogen sulfide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway methionine biosynthetic process Inferred from electronic annotation. Source: InterPro sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phosphoadenylyl-sulfate reductase (thioredoxin) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
groL	P0A6F5	1	EBI-1114555,EBI-543750

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5

Chain

2 – 244

243

Phosphoadenosine phosphosulfate reductase HAMAP-Rule MF_00063

PRO_0000100630

Experimental info

Mutagenesis

209

Y → F: Reduction in Vmax.

Mutagenesis

239

C → S: 5-fold reduction in Vmax.

Sequence conflict

E → Q in AAA23652. Ref.2

Sequence conflict

226

A → S in AAA23652. Ref.2

Secondary structure

244

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P17854 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7EC494ED2437E469
Show »

FASTA

244

27,976

        10         20         30         40         50         60 
MSKLDLNALN ELPKVDRILA LAETNAELEK LDAEGRVAWA LDNLPGEYVL SSSFGIQAAV 

        70         80         90        100        110        120 
SLHLVNQIRP DIPVILTDTG YLFPETYRFI DELTDKLKLN LKVYRATESA AWQEARYGKL 

       130        140        150        160        170        180 
WEQGVEGIEK YNDINKVEPM NRALKELNAQ TWFAGLRREQ SGSRANLPVL AIQRGVFKVL 

       190        200        210        220        230        240 
PIIDWDNRTI YQYLQKHGLK YHPLWDEGYL SVGDTHTTRK WEPGMAEEET RFFGLKRECG 


LHEG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli." Krone F.A., Westphal G., Schwenn J.D. Mol. Gen. Genet. 225:314-319(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase." Ostrowski J., Wu J.-Y., Rueger D.C., Miller B.E., Siegel L.M., Kredich N.M. J. Biol. Chem. 264:15726-15737(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"PAPS-reductase of Escherichia coli. Correlating the N-terminal amino acid sequence with the DNA of gene cys H." Krone F.A., Westphal G., Meyer H.E., Schwenn J.D. FEBS Lett. 260:6-9(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-18.
[6]	"Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis." Berendt U., Haverkamp T., Prior A., Schwenn J.D. Eur. J. Biochem. 233:347-356(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS.
[7]	"Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases." Savage H., Montoya G., Svensson C., Schwenn J.D., Sinning I. Structure 5:895-906(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

RDECPA. S14221.

RefSeq

NP_417242.1. NC_000913.2.
YP_490971.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SUR	X-ray	2.00	A	2-216	[»]
2O8V	X-ray	3.00	A	1-244	[»]

ProteinModelPortal

P17854.

SMR

P17854. Positions 2-244.

ModBase

Search...

Protein-protein interaction databases

IntAct

P17854. 4 interactions.

STRING

511145.b2762.

Proteomic databases

PaxDb

P17854.

PRIDE

P17854.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75804; AAC75804; b2762.
BAE76839; BAE76839; BAE76839.

GeneID

12932457.
947230.

KEGG

ecj:Y75_p2700.
eco:b2762.

PATRIC

32120936. VBIEscCol129921_2860.

Organism-specific databases

EchoBASE

EB0186.

EcoGene

EG10189. cysH.

Phylogenomic databases

eggNOG

COG0175.

HOGENOM

HOG000249396.

K00390.

OMA

WVDTGYL.

ProtClustDB

PRK02090.

Enzyme and pathway databases

BioCyc

EcoCyc:PAPSSULFOTRANS-MONOMER.
ECOL316407:JW2732-MONOMER.
MetaCyc:PAPSSULFOTRANS-MONOMER.

UniPathway

UPA00140; UER00206.

Gene expression databases

Genevestigator

P17854.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

HAMAP

MF_00063. CysH.

InterPro

IPR004511. PAPS/APS_Rdtase.
IPR002500. PAPS_reduct.
IPR011800. PAPS_reductase_CysH.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Pfam

PF01507. PAPS_reduct. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00434. cysH. 1 hit.
TIGR02057. PAPS_reductase. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P17854.

Entry information

Entry name

CYSH_ECOLI

Accession

Primary (citable) accession number: P17854
Secondary accession number(s): Q2MA67

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents