TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


3.D.4.3.3
Cbb3 cytochrome c oxidase (COX; Cbb3; CcoNOP).  The 3-d structure is known to 3.2 Å resolution (PDB# 3MK7; 5DJQ) (Buschmann et al. 2010Lee et al., 2012).  The structure explains a proton-pumping mechanism and the high activity of family-C heme-copper oxidases compared to that of families A and B (Buschmann et al., 2010Lee et al., 2012). A small subunit of 36 aas and 1 TMS, CcoM, was identified in the structure and plays a role in assembly and stability (Kohlstaedt et al. 2016; Carvalheda and Pisliakov 2017). CcoQ, another small protein of 62 aas (acc # F8H837) is an assembly factor for Cbb3-1 and Cbb3-2 (Kohlstaedt et al. 2017). The A-, B- and C-type oxygen reductases each have an active-site tyrosine that forms a unique cross-linked histidine-tyrosine cofactor. In the C-type oxygen reductases (also called cbb3 oxidases), this post-translationally generated co-factor occurs in a different TMS than for the A- and B-type reductases (Hemp et al. 2006).

Accession Number:F8H841
Protein Name:Cbb3-type cytochrome c oxidase subunit II
Length:203
Molecular Weight:22812.00
Species:Pseudomonas stutzeri (strain ATCC 17588 / DSM 5190 / CCUG 11256 / JCM 5965 / LMG 11199 / NCIMB 11358 / Stanier 221) [96563]
Number of TMSs:1
Substrate hydron, proton

Cross database links:

Entrez Gene ID: 10942783   
Pfam: PF02433   
KEGG: psz:PSTAB_1740   

Gene Ontology

GO:0009055 F:electron carrier activity
GO:0020037 F:heme binding

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MKSHEKLEKN VGLLTLFMIL AVSIGGLTQI VPLFFQDSVN EPVEGMKPYT ALQLEGRDLY 
61:	IREGCVGCHS QMIRPFRAET ERYGHYSVAG ESVYDHPFLW GSKRTGPDLA RVGGRYSDDW 
121:	HRAHLYNPRN VVPESKMPSY PWLVENTLDG KDTAKKMSAL RMLGVPYTEE DIAGARDSVN 
181:	GKTEMDAMVA YLQVLGTALT NKR