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    cysH phosphoadenosine phosphosulfate reductase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947230, updated on 17-Dec-2024

    Summary

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    Official Symbol
    cysH
    Official Full Name
    phosphoadenosine phosphosulfate reductase
    Primary source
    ECOCYC:EG10189
    Locus tag
    b2762
    See related
    ASAP:ABE-0009057
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK2757
    Summary
    PAPS reductase is composed of two identical subunits of 28 kDa. [More information is available at EcoCyc: EG10189].
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    Genomic context

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    Sequence:
    NC_000913.3 (2887578..2888312, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene CRISPR-associated endonuclease/helicase Cas3 Neighboring gene ncRNA Neighboring gene sulfite reductase, hemoprotein subunit Neighboring gene sulfite reductase, flavoprotein subunit

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. PAPS-reductase of Escherichia coli. Correlating the N-terminal amino acid sequence with the DNA of gene cys H. Krone FA, et al. FEBS Lett, 1990 Jan 15. PMID 2404794
    2. Pharmacokinetic and pharmacodynamic effects of high-dose continuous intravenous verapamil infusion: clinical experience in the intensive care unit. De Cicco M, et al. Crit Care Med, 1999 Feb. PMID 10075058
    3. New thioredoxins and glutaredoxins as electron donors of 3'-phosphoadenylylsulfate reductase. Lillig CH, et al. J Biol Chem, 1999 Mar 19. PMID 10075658
    4. Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli. Krone FA, et al. Mol Gen Genet, 1991 Feb. PMID 2005873
    5. Sulfate assimilation pathway intermediate phosphoadenosine 59-phosphosulfate acts as a signal molecule affecting production of curli fibres in Escherichia coli. Rossi E, et al. Microbiology (Reading), 2014 Sep. PMID 24934621

    See all (22) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Inactivation of the cysH gene results in increased surface adhesion and cell aggregation by activating the expression of the curli-encoding csgBAC operon via phosphoadenosine 59-phosphosulfate accumulation.
      Title: Sulfate assimilation pathway intermediate phosphoadenosine 59-phosphosulfate acts as a signal molecule affecting production of curli fibres in Escherichia coli.
    2. N-terminus verified by Edman degradation on mature peptide
      Title: PAPS-reductase of Escherichia coli. Correlating the N-terminal amino acid sequence with the DNA of gene cys H.
    3. the structure of PAPS reductase in complex with thioredoxin highlights the large structural rearrangement required to accomplish sulfonucleotide reduction and suggests a role for Trx in catalysis beyond the paradigm of disulfide reduction.
      Title: 3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables phosphoadenylyl-sulfate reductase (thioredoxin) activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables phosphoadenylyl-sulfate reductase (thioredoxin) activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables phosphoadenylyl-sulfate reductase (thioredoxin) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables phosphoadenylyl-sulfate reductase (thioredoxin) activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in hydrogen sulfide biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within sulfur compound metabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    phosphoadenosine phosphosulfate reductase
    NP_417242.1

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      2887578..2888312 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417242.1 phosphoadenosine phosphosulfate reductase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417242.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9ASU8
      Conserved Domains (1) summary
      PRK02090
      Location:6 → 244
      PRK02090; phosphoadenylyl-sulfate reductase
    Nucleotide Protein
    Heading Accession and Version

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