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ECOLI:CYSH

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) cysH
Protein Name(s) Phosphoadenosine phosphosulfate reductase

3'-phosphoadenylylsulfate reductase PAPS reductase, thioredoxin dependent PAPS sulfotransferase PAdoPS reductase

External Links
UniProt P17854
EMBL Y07525
M23008
U29579
U00096
AP009048
PIR S14221
RefSeq NP_417242.1
WP_000039850.1
PDB 1SUR
2O8V
PDBsum 1SUR
2O8V
ProteinModelPortal P17854
SMR P17854
BioGrid 4261451
IntAct P17854
STRING 511145.b2762
EPD P17854
PaxDb P17854
PRIDE P17854
EnsemblBacteria AAC75804
BAE76839
GeneID 947230
KEGG ecj:JW2732
eco:b2762
PATRIC 32120936
EchoBASE EB0186
EcoGene EG10189
eggNOG ENOG4105ET3
COG0175
HOGENOM HOG000249396
InParanoid P17854
KO K00390
OMA PRNKLLD
OrthoDB EOG6V1M7D
PhylomeDB P17854
BioCyc EcoCyc:PAPSSULFOTRANS-MONOMER
ECOL316407:JW2732-MONOMER
MetaCyc:PAPSSULFOTRANS-MONOMER
BRENDA 1.8.4.8
UniPathway UPA00140
EvolutionaryTrace P17854
PRO PR:P17854
Proteomes UP000000318
UP000000625
GO GO:0005737
GO:0004604
GO:0019344
GO:0070814
GO:0009086
GO:0019379
GO:0006790
Gene3D 3.40.50.620
HAMAP MF_00063
InterPro IPR004511
IPR002500
IPR011800
IPR014729
Pfam PF01507
PIRSF PIRSF000857
TIGRFAMs TIGR00434
TIGR02057

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0019379

sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10189
PANTHER:PTN000591370
SGD:S000006371

P

Seeded From UniProt

complete

GO:0004604

phosphoadenylyl-sulfate reductase (thioredoxin) activity

PMID:7588765[2]

ECO:0000315

F

From table 1, the significant reduction of Vmax quantities in both the mutant Cys236Ser and the Tyr206Phe enzymes compared to the wild type Vmax suggests that wild type cysH protein reduces phosphoadenylyl-sulfate.

complete
CACAO 11581

enables

GO:0004604

phosphoadenylyl-sulfate reductase (thioredoxin) activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10189
PANTHER:PTN000591370
SGD:S000006371
UniProtKB:P56859

F

Seeded From UniProt

complete

involved_in

GO:0019379

sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)

PMID:7588765[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006790

sulfur compound metabolic process

PMID:7588765[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004604

phosphoadenylyl-sulfate reductase (thioredoxin) activity

PMID:7588765[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002500

F

Seeded From UniProt

complete

enables

GO:0004604

phosphoadenylyl-sulfate reductase (thioredoxin) activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004511
InterPro:IPR011800

F

Seeded From UniProt

complete

involved_in

GO:0019379

sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004511
InterPro:IPR011800

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004511

P

Seeded From UniProt

complete

enables

GO:0004604

phosphoadenylyl-sulfate reductase (thioredoxin) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.8.4.8

F

Seeded From UniProt

complete

enables

GO:0004604

phosphoadenylyl-sulfate reductase (thioredoxin) activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000037451

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000037451

C

Seeded From UniProt

complete

involved_in

GO:0019379

sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000037451

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0070814

hydrogen sulfide biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00140

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 Berendt, U et al. (1995) Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Eur. J. Biochem. 233 347-56 PubMed GONUTS page