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P18408 (MET16_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoadenosine phosphosulfate reductase

EC=1.8.4.8
Alternative name(s):
3'-phosphoadenylylsulfate reductase
PAPS reductase, thioredoxin dependent
PAdoPS reductase
Gene names
Name:MET16
Ordered Locus Names:YPR167C
ORF Names:P9325.8
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The NADP dependent reduction of PAPS into sulfite involves thioredoxin which probably plays the role of a thiol carrier.

Catalytic activity

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

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 3/3.

Miscellaneous

Present with 217 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the PAPS reductase family. CysH subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRX1P222171EBI-11481,EBI-19607

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261Phosphoadenosine phosphosulfate reductase
PRO_0000100662

Experimental info

Sequence conflict242 – 26120KTECG…LKQDA → RPSVEFMKPADSRNF in AAA34774. Ref.1

Secondary structure

....................................................... 261
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18408 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 202AF2C20829513C

FASTA26130,380
        10         20         30         40         50         60 
MKTYHLNNDI IVTQEQLDHW NEQLIKLETP QEIIAWSIVT FPHLFQTTAF GLTGLVTIDM 

        70         80         90        100        110        120 
LSKLSEKYYM PELLFIDTLH HFPQTLTLKN EIEKKYYQPK NQTIHVYKPD GCESEADFAS 

       130        140        150        160        170        180 
KYGDFLWEKD DDKYDYLAKV EPAHRAYKEL HISAVFTGRR KSQGSARSQL SIIEIDELNG 

       190        200        210        220        230        240 
ILKINPLINW TFEQVKQYID ANNVPYNELL DLGYRSIGDY HSTQPVKEGE DERAGRWKGK 

       250        260 
AKTECGIHEA SRFAQFLKQD A 

« Hide

References

« Hide 'large scale' references
[1]"Gene-enzyme relationship in the sulfate assimilation pathway of Saccharomyces cerevisiae. Study of the 3'-phosphoadenylylsulfate reductase structural gene."
Thomas D., Barbey R., Surdin-Kerjan Y.
J. Biol. Chem. 265:15518-15524(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05591 Genomic DNA. Translation: AAA34774.1.
U25840 Genomic DNA. Translation: AAB68154.1.
AY693236 Genomic DNA. Translation: AAT93255.1.
BK006949 Genomic DNA. Translation: DAA11584.1.
PIRS59826.
RefSeqNP_015493.1. NM_001184264.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OQ2X-ray2.10A/B/C/D1-261[»]
ProteinModelPortalP18408.
SMRP18408. Positions 1-257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36340. 49 interactions.
DIPDIP-6611N.
MINTMINT-677033.
STRING4932.YPR167C.

Proteomic databases

PaxDbP18408.
PeptideAtlasP18408.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPR167C; YPR167C; YPR167C.
GeneID856296.
KEGGsce:YPR167C.

Organism-specific databases

CYGDYPR167c.
SGDS000006371. MET16.

Phylogenomic databases

eggNOGCOG0175.
HOGENOMHOG000249397.
KOK00390.
OMAPRNKLLD.
OrthoDBEOG7P2Z3B.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-384.
YEAST:YPR167C-MONOMER.
UniPathwayUPA00140; UER00206.

Gene expression databases

GenevestigatorP18408.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
InterProIPR004511. PAPS/APS_Rdtase.
IPR002500. PAPS_reduct.
IPR011800. PAPS_reductase_CysH.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF01507. PAPS_reduct. 1 hit.
[Graphical view]
PIRSFPIRSF000857. PAPS_reductase. 1 hit.
TIGRFAMsTIGR00434. cysH. 1 hit.
TIGR02057. PAPS_reductase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP18408.
NextBio981647.
PROP18408.

Entry information

Entry nameMET16_YEAST
AccessionPrimary (citable) accession number: P18408
Secondary accession number(s): D6W4G8, Q06212
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1997
Last modified: February 19, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways