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    cydA cytochrome bd-I subunit 1 [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945341, updated on 3-Dec-2024

    Summary

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    Official Symbol
    cydA
    Official Full Name
    cytochrome bd-I subunit 1
    Primary source
    ECOCYC:EG10173
    Locus tag
    b0733
    See related
    ASAP:ABE-0002499
    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
    cyd-1; ECK0721
    Summary
    H-NS, Fnr and ArcA regulons. [More information is available at EcoGene: EG10173]. CydA contains the heme b558 component of cytochrome bd-I . [More information is available at EcoCyc: EG10173].
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    Genomic context

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    Sequence:
    NC_000913.3 (771458..773026)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene 2-O-alpha-mannosyl-D-glycerate specific PTS enzyme II Neighboring gene alpha-mannosidase Neighboring gene cytochrome bd-I subunit 2 Neighboring gene cytochrome bd-I accessory subunit CydX Neighboring gene PF09600 family protein YbgE

    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. Cytochrome bd-I from Escherichia coli is catalytically active in the absence of the CydH subunit. Goojani HG, et al. FEBS Lett, 2023 Feb. PMID 36460943
    2. Isolation and characterization of an Escherichia coli mutant lacking cytochrome d terminal oxidase. Green GN, et al. J Bacteriol, 1983 Jun. PMID 6304009, Free PMC Article
    3. Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli. Kaysser TM, et al. Biochemistry, 1995 Oct 17. PMID 7577938
    4. Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site. Belevich I, et al. Proc Natl Acad Sci U S A, 2005 Mar 8. PMID 15728392, Free PMC Article
    5. Site-directed mutation of the highly conserved region near the Q-loop of the cytochrome bd quinol oxidase from Escherichia coli specifically perturbs heme b595. Zhang J, et al. Biochemistry, 2001 Jul 24. PMID 11456494

    See all (88) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Cytochrome bd-I from Escherichia coli is catalytically active in the absence of the CydH subunit.
      Title: Cytochrome bd-I from Escherichia coli is catalytically active in the absence of the CydH subunit.
    2. structure of the E. coli cytochrome bd-I oxidase to a resolution of 2.7 angstroms; structure contains an accessory subunit CydH encoded by ynhF, the L-subfamily-specific Q-loop domain, a structural ubiquinone-8 cofactor, an active-site density interpreted as dioxygen, distinct water-filled proton channels, and an oxygen-conducting pathway
      Title: Active site rearrangement and structural divergence in prokaryotic respiratory oxidases.
    3. Cytochrome bd oxidases split the O-O bond in a single four-electron transfer reaction without a peroxide intermediate.
      Title: Oxoferryl-porphyrin radical catalytic intermediate in cytochrome bd oxidases protects cells from formation of reactive oxygen species.
    4. Removal of three terminal cytochrome oxidase genes (cydAB, cyoABCD, and cbdAB) and a quinol monooxygenase gene (ygiN) from the Escherichia coli K-12 MG1655 genome resulted in the activation of ArcA aerobically.
      Title: Deletion of genes encoding cytochrome oxidases and quinol monooxygenase blocks the aerobic-anaerobic shift in Escherichia coli K-12 MG1655.
    5. E. coli can compensate for the loss of cytochrome bd-I activity and cytochrome bd-II-mediated quinol oxidation prevents the accumulation of NADH
      Title: Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism.
    6. The data support models of the catalytic cycle which do not include the fully oxidized form of cytochrome bd quinol oxidase as an intermediate.
      Title: The fully oxidized form of the cytochrome bd quinol oxidase from E. coli does not participate in the catalytic cycle: direct evidence from rapid kinetics studies.
    7. N-terminus verified by Edman degradation on complete protein
      Title: Oxidative protein folding is driven by the electron transport system.
    Submit: New GeneRIF Correction

    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 electron transfer activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables electron transfer activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables electron transfer activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables heme binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables heme binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables heme binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity, acting on diphenols and related substances as donors IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in aerobic electron transport chain IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within aerobic electron transport chain IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in aerobic electron transport chain IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in aerobic electron transport chain NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in oxidative phosphorylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in oxidative phosphorylation NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of cytochrome complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of cytochrome complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of cytochrome complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of cytochrome complex IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    located_in membrane HDA PubMed 
    located_in membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in plasma membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in plasma membrane ISM
    Inferred from Sequence Model
    more info
    		 PubMed 
    located_in plasma membrane RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    cytochrome bd-I subunit 1
    NP_415261.2

    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
      771458..773026
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415261.2 cytochrome bd-I subunit 1 [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415261.2

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376MAL1
      Conserved Domains (1) summary
      PRK15097
      Location:1 → 522
      PRK15097; cytochrome bd-I ubiquinol oxidase subunit CydA
    Nucleotide Protein
    Heading Accession and Version

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