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virulence, detoxification, adaptation
information pathways
cell wall and cell processes
stable RNAs
insertion seqs and phages
PE/PPE
intermediary metabolism and respiration
unknown
regulatory proteins
conserved hypotheticals
lipid metabolism
pseudogenes
General annotation
TypeCDS
FunctionCytochrome C oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome C are transferred via the copper a center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme A3 and copper B [catalytic activity: 4 ferrocytochrome C + O(2) = 2 H(2)O + 4 ferricytochrome C].
ProductProbable cytochrome C oxidase polypeptide I CtaD (cytochrome AA3 subunit 1)
CommentsRv3043c, (MTV012.58c), len: 573 aa. Probable ctaD, integral membrane cytochrome C oxidase polypeptide I, equivalent to Q9CBQ5|ML1728 from Mycobacterium leprae (574 aa), FASTA scores: opt: 3738, E(): 3.8e-216, (95.4% identity in 566 aa overlap). Also similar to other cytochrome C oxidases polypeptide I e.g. Q9AEL9|CTAD from Corynebacterium glutamicum (Brevibacterium flavum) (584 aa), FASTA scores: opt: 3065, E(): 6.8e-176, (72.65% identity in 567 aa overlap); Q9X813|SC6G10.28c from Streptomyces coelicolor (578 aa), FASTA scores: opt: 2888, E(): 2.6e-165, (71.7% identity in 544 aa overlap); Q9K451|CTAD from Streptomyces coelicolor (573 aa), FASTA scores: opt: 2757, E(): 1.8e-157, (70.2% identity in 537 aa overlap). Contains PS00077 Cytochrome c oxidase subunit I, copper B binding region signature. Belongs to the heme-copper respiratory oxidase family.
Functional categoryIntermediary metabolism and respiration
ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using nanoLC-MS/MS; predicted integral membrane protein (See Xiong et al., 2005). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in M. tuberculosis H37Rv-infected guinea pig lungs at 30 days but not 90 days (See Kruh et al., 2010). Identified by mass spectrometry in the membrane protein fraction of M. tuberculosis H37Rv but not the culture filtrate or membrane protein fraction (See de Souza et al., 2011).
MutantEssential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Essential gene by Himar1 transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011).
Check for mutants available at TARGET website
Coordinates
TypeStartEndOrientation
CDS34032003404921-
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3043c|ctaD
LTAEAPPLGELEAIRPYPARTGPKGSLVYKLITTTDHKMIGIMYCVACISFFFIGGLLALLMRTELAAPGLQFLSNEQFNQLFTMHGTIMLLFYATPIVFGFANLVLPLQIGAPDVAFPRLNAFSFWLFVFGATIGAAGFITPGGAADFGWTAYTPLTDAIHSPGAGGDLWIMGLIVAGLGTILGAVNMITTVVCMRAPGMTMFRMPIFTWNIMVTSILILIAFPLLTAALFGLAADRHLGAHIYDAANGGVLLWQHLFWFFGHPEVYIIALPFFGIVSEIFPVFSRKPIFGYTTLVYATLSIAALSVAVWAHHMFATGAVLLPFFSFMTYLIAVPTGIKFFNWIGTMWKGQLTFETPMLFSVGFMVTFLLGGLTGVLLASPPLDFHVTDSYFVVAHFHYVLFGTIVFATFAGIYFWFPKMTGRLLDERLGKLHFWLTFIGFHTTFLVQHWLGDEGMPRRYADYLPTDGFQGLNVVSTIGAFILGASMFPFVWNVFKSWRYGEVVTVDDPWGYGNSLEWATSCPPPRHNFTELPRIRSERPAFELHYPHMVERLRAEAHVGRHHDEPAMVTSS