Phosphoadenosine phosphosulfate reductase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P17854 (CYSH_ECOLI)

Last modified June 16, 2009. Version 89. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Phosphoadenosine phosphosulfate reductase
    EC=1.8.4.8
Alternative name(s):
    PAPS reductase, thioredoxin dependent
    PAdoPS reductase
    3'-phosphoadenylylsulfate reductase
    PAPS sulfotransferase

Gene names

Name:	cysH
Ordered Locus Names:	b2762, JW2732

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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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.

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General annotation (Comments)

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

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Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cysteine biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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 protein binding Inferred from physical interaction. Source: IntAct transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

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

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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 MF_00063

PRO_0000100630

Experimental info

Mutagenesis

209

Y → F: Reduction in Vmax. HAMAP MF_00063

Mutagenesis

239

C → S: 5-fold reduction in Vmax. HAMAP MF_00063

Sequence conflict

E → Q in AAA23652. Ref.2

Sequence conflict

226

A → S in AAA23652. Ref.2

Secondary structure

244

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P17854-1 [UniParc].

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

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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: 2005873] [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: 2670946] [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: 9278503] [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: 16738553] [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: 2404794] [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: 7588765] [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: 9261082] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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

AP_003329.1.
NP_417242.1.

3D structure databases

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P17854. 4 interactions.

Genome annotation databases

GeneID

947230.

GenomeReviews

Gene locus JW2732 in contig AP009048_GR.
Gene locus b2762 in contig U00096_GR.

KEGG

ecj:JW2732.
eco:b2762.

Organism-specific databases

EchoBASE

EB0186.

EcoGene

EG10189. cysH.

CMR

Search...

Phylogenomic databases

HOGENOM

P17854.

OMA

P17854. TRFNGLK.

Enzyme and pathway databases

BioCyc

EcoCyc:PAPSSULFOTRANS-MON.
MetaCyc:PAPSSULFOTRANS-MON.

Family and domain databases

HAMAP

MF_00063.
[Tree]

InterPro

IPR004511. PAdo_PSO4_Rdtase_CysH.
IPR002500. PAPS_reduct.
IPR011800. PAPS_reductase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Gene3D

G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.

Pfam

PF01507. PAPS_reduct. 1 hit.
[Graphical view]

TIGRFAMs

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

ProtoNet

Search...

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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:	June 16, 2009
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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 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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents