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A0A1V6PRF5 A0A1V6PRF5 A0A1V6PT23 A0A1V6PT23 A0A1V6PUS1 A0A1V6PUS1 A0A1V6PW04 A0A1V6PW04 A0A1V6PW46 A0A1V6PW46 A0A1V6PXQ8 A0A1V6PXQ8 BNA5-2 BNA5-2 A0A1V6PQ74 A0A1V6PQ74 BNA5 BNA5 A0A1V6Q1I3 A0A1V6Q1I3 A0A1V6Q2P4 A0A1V6Q2P4 A0A1V6Q7Q8 A0A1V6Q7Q8 A0A1V6Q7T5 A0A1V6Q7T5 A0A1V6QAW1 A0A1V6QAW1 A0A1V6QCJ5 A0A1V6QCJ5 A0A1V6QCM3 A0A1V6QCM3 A0A1V6QDC3 A0A1V6QDC3 BNA4 BNA4 A0A1V6QDK0 A0A1V6QDK0 A0A1V6QHA3 A0A1V6QHA3 BNA1 BNA1 A0A1V6QIJ0 A0A1V6QIJ0 A0A1V6QKX2 A0A1V6QKX2
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
A0A1V6PRF5Uncharacterized protein. (606 aa)
A0A1V6PT23NAD(P)H-hydrate epimerase; Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. (237 aa)
A0A1V6PUS1Uncharacterized protein. (424 aa)
A0A1V6PW04RED_N domain-containing protein. (535 aa)
A0A1V6PW46Nicotinamide-nucleotide adenylyltransferase; Belongs to the eukaryotic NMN adenylyltransferase family. (281 aa)
A0A1V6PXQ8ATP-dependent (S)-NAD(P)H-hydrate dehydratase; Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S-and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Belongs to the NnrD/CARKD family. (368 aa)
BNA5-2Kynureninase; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively; Belongs to the kynureninase family. (485 aa)
A0A1V6PQ74Uncharacterized protein. (416 aa)
BNA5Kynureninase; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively; Belongs to the kynureninase family. (464 aa)
A0A1V6Q1I3Nicotinate phosphoribosyltransferase; Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP; Belongs to the NAPRTase family. (467 aa)
A0A1V6Q2P4Uncharacterized protein; Belongs to the alkaline phosphatase family. (662 aa)
A0A1V6Q7Q8CTP_transf_like domain-containing protein. (297 aa)
A0A1V6Q7T5Glutamine-dependent NAD(+) synthetase; In the C-terminal section; belongs to the NAD synthetase family. (709 aa)
A0A1V6QAW1Purine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. (310 aa)
A0A1V6QCJ5Uncharacterized protein. (514 aa)
A0A1V6QCM3Uncharacterized protein. (645 aa)
A0A1V6QDC3IU_nuc_hydro domain-containing protein. (372 aa)
BNA4Kynurenine 3-monooxygenase; Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid. (511 aa)
A0A1V6QDK0Alkaline phosphatase. (600 aa)
A0A1V6QHA3Nudix hydrolase domain-containing protein. (439 aa)
BNA13-hydroxyanthranilate 3,4-dioxygenase; Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate. (187 aa)
A0A1V6QIJ0Nicotinate-nucleotide pyrophosphorylase [carboxylating]; Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family. (291 aa)
A0A1V6QKX2Uncharacterized protein. (473 aa)
Your Current Organism:
Penicillium antarcticum
NCBI taxonomy Id: 416450
Other names: CBS 100492, FRR 4989, P. antarcticum
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