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cbaA ba3-type cytochrome C oxidase subunit I [ Thermus thermophilus HB8 ]

Gene ID: 3168993, updated on 12-Feb-2024

Summary

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Gene symbol
cbaA
Gene description
ba3-type cytochrome C oxidase subunit I
Locus tag
TTH_RS05765
Gene type
protein coding
Organism
Thermus thermophilus HB8 (strain: HB8, type-material: type strain of Thermus thermophilus)
Lineage
Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus
Old locus tag
TTHA1135
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Genomic context

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Location:
chromosome: 1
Sequence:
Chromosome: 1; NC_006461.1 (1076139..1077827)

Chromosome 1 - NC_006461.1Genomic Context describing neighboring genes Neighboring gene ctochrome c oxidase polypeptide 2A Neighboring gene ba3-type cytochrome C oxidase subunit II Neighboring gene hypothetical protein Neighboring gene MFS transporter Neighboring gene 30S ribosomal protein S15

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_006461.1

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. All the O2 Consumed by Thermus thermophilus Cytochrome ba3 Is Delivered to the Active Site through a Long, Open Hydrophobic Tunnel with Entrances within the Lipid Bilayer. Mahinthichaichan P, et al. Biochemistry, 2016 Mar 1. PMID 26845082, Free PMC Article
  2. The structure of a ferrous heme-nitro species in the binuclear heme a3/CuB center of ba3-cytochrome c oxidase as determined by resonance Raman spectroscopy. Loullis A, et al. Chem Commun (Camb), 2015. PMID 25406996
  3. Single mutations that redirect internal proton transfer in the ba3 oxidase from Thermus thermophilus. Smirnova I, et al. Biochemistry, 2013 Oct 8. PMID 24004023, Free PMC Article
  4. Probing protonation/deprotonation of tyrosine residues in cytochrome ba3 oxidase from Thermus thermophilus by time-resolved step-scan Fourier transform infrared spectroscopy. Koutsoupakis C, et al. J Biol Chem, 2011 Sep 2. PMID 21757723, Free PMC Article
  5. The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase. A combined NMR and computational approach. Muresanu L, et al. J Biol Chem, 2006 May 19. PMID 16554303

See all (14) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Results indicatethe importance of valine 236 (V236) in facilitating access of ligands to the active site in ba3 cytochrome oxidase.
    Title: Role of the Conserved Valine 236 in Access of Ligands to the Active Site of Thermus thermophilus ba(3) Cytochrome Oxidase.
  2. O2 diffuses to the active site of Cytochrome ba3 exclusively via a Y-shaped hydrophobic tunnel with two 25-A long membrane-accessible branches.
    Title: All the O2 Consumed by Thermus thermophilus Cytochrome ba3 Is Delivered to the Active Site through a Long, Open Hydrophobic Tunnel with Entrances within the Lipid Bilayer.
  3. Characterized is a ferrous heme a3-nitro species in ba3-cytochrome c oxidase by resonance Raman spectroscopy. This provides the first evidence for the structure of a nitrite-bound species in the binuclear heme/copper center of cytochrome c oxidases.
    Title: The structure of a ferrous heme-nitro species in the binuclear heme a3/CuB center of ba3-cytochrome c oxidase as determined by resonance Raman spectroscopy.
  4. Thr312Val and Tyr244Phe mutations interfere with a structural rearrangement in the proton pathway that is rate limiting for proton transfer to the catalytic site.
    Title: Single mutations that redirect internal proton transfer in the ba3 oxidase from Thermus thermophilus.
  5. X-ray crystallography and site directed mutagenesis reveal details of ligand access to the active site of a bacterial cytochrome oxidase.
    Title: Ligand access to the active site in Thermus thermophilus ba(3) and bovine heart aa(3) cytochrome oxidases.
  6. Studies indicate that the ba(3) cytochrome c oxidase pump protons with a lower stoichiometry of 0.5 H(+)/electron and use only one proton pathway for the transfer of all protons.
    Title: Proton transfer in ba(3) cytochrome c oxidase from Thermus thermophilus.
  7. Data show that a fraction of cytochrome ba(3) (ba(3)) decayed to the oxidized state within the dead time (~1ms), while the remaining amount was in a reduced state that decayed slowly to the oxidized state without accumulation of detectable intermediates.
    Title: The rate-limiting step in O(2) reduction by cytochrome ba(3) from Thermus thermophilus.
  8. Data indicate that the Crystal structures of CO-bound cytochrome ba(3)-oxidase reveal a Fe-C distance of ~2.0A, a Cu-O distance of 2.4A and a Fe-C-O angle of ~126 degrees .
    Title: Structural changes that occur upon photolysis of the Fe(II)(a3)-CO complex in the cytochrome ba(3)-oxidase of Thermus thermophilus: a combined X-ray crystallographic and infrared spectral study demonstrates CO binding to Cu(B).
  9. Studies indicate that the ba(3)-oxidase structure has provided evolutionary and functional information.
    Title: Bioenergetics at extreme temperature: Thermus thermophilus ba(3)- and caa(3)-type cytochrome c oxidases.
  10. Studies indicate that nitric oxide (NO) binding to reduced ba(3) and bovine cytochrome aa3.
    Title: Kinetic studies of the reactions of O(2) and NO with reduced Thermus thermophilus ba(3) and bovine aa(3) using photolabile carriers.
Submit: New GeneRIF Correction See all GeneRIFs (12)

General protein information

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Preferred Names
ba3-type cytochrome C oxidase subunit I
WP_011173204.1

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_006461.1 Reference assembly

    Range
    1076139..1077827
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. WP_011173204.1 MULTISPECIES: ba3-type cytochrome C oxidase subunit I [Thermus]

    See identical proteins and their annotated locations for WP_011173204.1

    UniProtKB/Swiss-Prot
    Q5SJ79
    UniProtKB/TrEMBL
    A0A7R7TDX5, Q72JK2
    Conserved Domains (1) summary
    cd01660
    Location:16 → 493
    ba3-like_Oxidase_I; ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the ...
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
1EHK_A.1
Q5SJ79.1

Gene LinkOut

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