Phaeodactylum tricornutum CCAP 1055/1 chromosome 20, 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 CM000622.\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##
Carbamoyl-phosphate synthase II is the first step of the UTP biosynthetic pathway.
This predicted protein belongs to a family that contains nitrilases that break carbon-nitrogen bonds and appear to be involved in the reduction of organic nitrogen compounds and ammonia production. They all have distinct substrate specificity and include cyanide hydratases, aliphatic amidases, beta-alanine synthase, and a few other proteins with unknown molecular function.; Acylamide amidohydrolase; Wide spectrum amidase
This dehydrogenase is close to D-lactate dehydrogenase || Most probably a 2-hydroxyacid dehyrdogenase, similar to D-lactate dehydrogenase, with NAD+ or NADP+ as acceptor. The model encodes for an N-terminal transcription factor domain of the CAP family, presumably activated by binding of an effector molecule.; 2-hydroxyacid dehydrogenase
Contains lipoprotein type 6 domain. Members of this family are likely involved in evasion of the host immune system by pathogens. Best hit to yeast Bfr1 (involved in mitosis and vesicular transport). EST evidence but little sequence similarity with other organisms.
Phosphoglycerate kinase that is probably targeted to the mitochondria (TargetP positive for mitochondria).
Hydrolyzes 1,3-beta-D-glucosyl residues.; glycosyl hydrolase family 16
protein fucoxanthin chlorophyll a/c protein
L-lactate transporter of bacterial origin. Highly expressed under conditions of nitrogen depletion.
pyruvate kinase, 21 residues at N-terminus predicted as mitochontrial transit peptide by targetp v1.1
Probably catalyzes the reaction: D-glucose 6-phosphate + NADP+ = D-glucono-1,5-lactone 6-phosphate + NADPH + H+
Kinesin-related motor protein, involved in microtubule-based motility
Membrane targeted ammonium transporter. This is one of eight ammonium transporters in the Pt genome. Phylogenetically, this transporter is very similar to the Pt transporter that is on scaffold 181.
Contains a ferric reductase-domain. Involved in reduction of ferric iron. Upstream and downstream UTRs. Multiple transmembrane domains.
unknown function; similarity to metallo-beta-lactamase superfamily protein; secretory pathway
unknown protein; highly expressed under iron starvation; secretory pathway
unknown function; weak similarity to GPI-anchored Fasciclin-like arabinogalactan protein; secretory pathway
cellular repressor of e1a-stimulated gene-like protein
small flavoprotein with acylphosphatase activity
threonine dehydratase. glycine, serine, threonine metabolism
DNA polymerase primase (p 49 small sub unit)
A short-chain dehydrogenase probably catalyzing the reaction: (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.
Similar to the Ohp proteins of Arabidopsis thaliana (one transmembrane helix)
Proteinase inhibitor, can be induced by leaf damage in plants.
Probable Acetate-CoA ligase ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA Also acts on propanoate and propenoate. Involved in Glycolysis / Gluconeogenesis, Pyruvate metabolism, Propanoate metabolism and Reductive carboxylate cycle (CO2 fixation)
A plastid enzyme, serves as E3 of pyruvate dehydrogenase complex, with the enzymes acting in concert to generate acetyl-CoA and NADH for de novo fatty acid synthesis. Catalyzes the reaction: dihydrolipoamide + NAD+ = lipoamide + NADH + H+, using FAD as a co-factor.
cytosolic pyruvate kinase, see also GenBank AY608679
fructose-1,6-bisphosphat aldolase, classII, plastidic isoenzyme, contains bipartite plastid targeting presequence, Genebank AAO43262
cytosolic pyruvate kinase, see also GenBank AY608678