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

Gene ID: 945341, updated on 19-Nov-2025
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
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; 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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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 Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. 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
  2. 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
  3. 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
  4. Glutamate 107 in subunit I of cytochrome bd from Escherichia coli is part of a transmembrane intraprotein pathway conducting protons from the cytoplasm to the heme b595/heme d active site. Borisov VB, et al. Biochemistry, 2008 Jul 29. PMID 18597483
  5. 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

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
Products Interactant Other Gene Complex Source Pubs Description

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 
Preferred Names
cytochrome bd-I subunit 1
NP_415261.2

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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

    See identical proteins and their annotated locations for NP_415261.2

    Status: REVIEWED

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