Phaeodactylum tricornutum CCAP 1055/1 chromosome 23, whole genome shotgun sequence.
Eukaryota; Stramenopiles; Bacillariophyta; Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae; Phaeodactylum.
The Phaeodactylum genome reveals the evolutionary history of diatom genomes
Submitted (15-JUN-2017) National Center for Biotechnology Information, NIH, Bethesda, MD 20894, USA
Submitted (12-AUG-2008) US DOE Joint Genome Institute, 2800 Mitchell Drive B100, Walnut Creek, CA 94598-1698, USA
PROVISIONAL REFSEQ: This record has not yet been subject to final\nNCBI review. The reference sequence is identical to CM000625.\nURL -- http://www.jgi.doe.gov/phaeodactylum\nJGI Project ID: 3634397\nContacts: Chris Bowler (cbowler@biologie.ens.fr)\n Igor Grigoriev (ivgrigoriev@lbl.gov)\nThe clone of P. tricornutum that was sequenced is CCAP1055/1 and is\navailable from the Culture collection of Algae and Protozoa\n(http://www.ccap.ac.uk). This clone represents a monoclonal culture\nderived from a fusiform cell in May 2003 from strain CCCP632, which\nwas originally isolated in 1956 off Blackpool (U.K.). It has been\nmaintained in culture continuously in F/2 medium.\nAnnotation was done by the JGI Annotation team and the Diatom\nConsortium.\nChromosomes 3 and 11 are complete and present in GenBank records\nCP001142 and CP001141, respectively.\nThe JGI and collaborators endorse the principles for the\ndistribution and use of large scale sequencing data adopted by the\nlarger genome sequencing community and urge users of this data to\nfollow them. It is our intention to publish the work of this\nproject in a timely fashion and we welcome collaborative\ninteraction on the project and analysis.\n(http://www.genome.gov/page.cfm?pageID=10506376)\nAnnotated scaffolds were added in December 2008.\n\n##Genome-Annotation-Data-START##\nAnnotation Provider :: INSDC submitter\nAnnotation Status :: Full annotation\nAnnotation Pipeline :: Eukaryotic Annotation Propagation Pipeline\n##Genome-Annotation-Data-END##
Hypothetical Cell death related protein, contains Programmed cell death protein 2, C-terminal Pfam domain and expressed exclusively under Ammonia starvation and toxic level of decadienal.
bifunctional enzyme involved in beta-oxidation of fatty acids. 3,2-trans-enoyl-CoA isomerase domain is required for beta-oxidation of unsaturated fatty acids. Converts (3S)-3-hydroxyacyl-CoA to trans-2(or 3)-enoyl-CoA + H(2)O, (S)-3-hydroxyacyl-CoA + NAD(+) to 3-oxoacyl-CoA + NADH, and 3-cis-enoyl-CoA to 2-trans-enoyl-CoA. Contains N- and C- terminal peroxisomal targeting motifs.; Enoyl-CoA hydratase
transcriptional activator of heat shock genes, located in cytosol/nucleus
Hypothetical protein with putative alanine glyoxylate aminotransferase domain; however, strong alignment with putative serine-pyruvate aminotransferase, an enzyme in the photorespiratory pathway that catalyzes the conversion of serine to hydroxypyruvate; DBGET notes that these two enzymes may be identical (EC 2.6.1.44 an
Involved in SUF system of FeS cluster assembly. 27% or more identical to cyanobacterial and proteobacterial sufD
Gene of unknown function contains domain for pathogenesis-related genes transcriptional activator and ethylene-responsive factors. Good EST coverage and homolog to T. pseudonana in the 3' end of the gene.
Hydrolyzes non-reducing terminal 1,3-beta-D-glucosyl residues.
seventh step in heme synthesis, originaly cytosolic enzyme, which now contains putative ER signal peptide at the N terminus; putatively chloroplast targeted
succinyl-coenzyme A:3-oxo-acid coenzyme a-transferase
A mitochondrial enzyme, catalyzes the reversible transfer of CoA between succinyl-CoA and another carboxylic acid in the reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA. A number of 3-oxo acids may serve as the acceptor but acetoacetate is the preferred substrate. Potential roles in synthesis and degradation of ketone bodies (in lipid metabolism), leucine degradation, and butanoate metabolism.
pyruvate kinase, 40 residues at N-terminus predicted as mitochontrial transit peptide by targetp v1.1
Macrophage migration inhibitory factor (MIF) seems to play an important role in host inflammatory responses where it is involved in the host response to endotoxic shock probably serving as a 'stress' hormone that regulates systemic inflammatory responses. MIF is a secreted protein.
Probable component of 2-oxoglutarate dehydrogenase complex TCA cycle: enzyme involved in succinate/2 oxoglutarate reaction. Also close to acetyltransferase component of pyruvate dehydrogenase
precursor of carboxylase pyruvate carboxylase
Replenishes the supply of oxaloacetate for the tricarboxylic acid cycle by catalyzing the reaction: pyruvate + ATP + HCO3- = oxaloacetate + ADP + Pi.
putative 5-methyltetrahydrofolate-homocysteine methyltransferase, vitamin B12 (or cobalamine)-dependent methionine synthase; located in cytosol
delta l-pyrroline-5-carboxylate synthetase
delta l-pyrroline-5-carboxylate synthetase contains a glutamate 5-kinase region followed by a gamma-glutamyl phosphate reductase region and catalyses the first and second steps in proline biosynthesis.Catalyses ATP + L-glutamate = ADP + L-glutamate 5-phosphate and L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl 5-phosphate + NADPH
contains conserved domain of unknown function; unknownn membrane protein