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StatusReference proteome
Proteinsi <p>Number of protein entries associated with this proteome: UniProtKB entries for regular proteomes or UniParc entries for redundant proteomes (<a href="/help/proteome%5Fredundancy">more...</a>)</p> 2,022
Gene counti <p>This is the total number of unique genes found in the proteome set, algorithmically computed. For each gene, a single representative protein sequence is chosen from the proteome. Where possible, reviewed (Swiss-Prot) protein sequences are chosen as the representatives.</p> - Download one protein sequence per gene (FASTA)
Proteome IDi <p>The proteome identifier (UPID) is the unique identifier assigned to the set of proteins that constitute the <a href="">proteome</a>. It consists of the characters 'UP' followed by 9 digits, is stable across releases and can therefore be used to cite a UniProt proteome.<p><a href='/help/proteome_id' target='_top'>More...</a></p>UP000000758
Taxonomy414004 - Cenarchaeum symbiosum (strain A)
Last modifiedDecember 1, 2019
Genome assembly and annotationi <p>Identifier for the genome assembly (<a href="">more...</a>)</p> GCA_000200715.1 from ENA/EMBL full

Cenarchaeum symbiosum is a psychrophilic nonthermophilic crenarchaeon symbiont of the marine sponge Axinella mexicana. It was isolated from coastal waters off Santa Barbara, CA. Crenarchaeota are ubiquitous and abundant microbial constituents of soils, sediments, lakes, and ocean waters. C. symbiosum genotypes coinhabiting the same host partitioned into two dominant populations, corresponding to previously described a- and b-type ribosomal RNA variants. Although they were syntenic, overlapping a- and b-type ribotype genomes harbored significant variability. A single tiling path comprising the dominant a-type genotype was assembled and used to explore the genomic properties of C. symbiosum. Its genome is remarkably distinct from those of other known Archaea and shares many core metabolic features in common with its free-living planktonic relatives. Multiple components of a putative CO2 assimilation pathway and enzymes involved in the oxidative tricarboxylic acid (TCA) cycle are present. Crenarchaeota appear to contain an intact form of the Embden-Meyerhof-Parnas (EMP) pathway for the metabolism of hexose sugars, which seems to function in the gluconeogenic direction rather than the glycolytic pathway. C. symbiosum does not use the Entner-Duodoroff (ED) pathway in the catabolism of hexose sugars. Homologues of genes potentially associated with chemolithotrophic ammonia oxidation, are represented in the C. symbiosum genome, but if it does indeed derive energy directly from ammonia oxidation, it appears to employ different mechanisms than typical nitrifying bacteria for oxidizing hydroxylamine. Genes required to synthesize all 20 amino acids with the exception of proline, are present. Nearly complete sets of genes required for the de novo synthesis of biotin, vitamin B12, riboflavin, thiamine, and pyridoxine were all identified. In the case of folic acid biosynthesis, genes encoding all steps for the conversion of the C1 carrier tetrahydrofolate (THF) to methyl-THF were identified. The full repertoire of genes necessary for chromosomal replication fork assembly and function also exist, and genes encoding two distinct DNA polymerases were identified. Viable and dividing populations of C. symbiosum have been observed to persist in a single sponge host individual for up to 5 years. As an apparently nonmotile extracellular symbiont, C. symbiosum likely has developed mechanisms to inhibit or evade host consumption and defend against viral predation. One possible interaction between Axinella and C. symbiosum is removal of nitrogenous host-waste products (e.g., ammonia, urea). This could simultaneously fuel the symbiont respiratory energy metabolism and might even provide new carbon to the host, via archaeal chemolithotrophic CO2 fixation, and subsequent symbiont-host carbon exchange.

Componentsi <p>Genomic components encoding the proteome</p>

Component nameGenome Accession(s)
Component representationProteins
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Main funding by: National Institutes of Health

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