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CAZyme Information: OAG24241.1

You are here: Home > Sequence: OAG24241.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Alternaria alternata
Lineage Ascomycota; Dothideomycetes; ; Pleosporaceae; Alternaria; Alternaria alternata
CAZyme ID OAG24241.1
CAZy Family GT1
CAZyme Description nicotinate-nucleotide diphosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
690 KV441471|CGC7 74520.74 5.4038
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AalternataSRC1lrK2f 13577 N/A 111 13466
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in OAG24241.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH16 382 649 1e-76 0.9563318777292577

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
185690 GH16_fungal_Lam16A_glucanase 2.76e-133 333 670 1 293
fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Group of fungal 1,3(4)-beta-D-glucanases, similar to Phanerochaete chrysosporium laminarinase 16A. Lam16A belongs to the 'nonspecific' 1,3(4)-beta-glucanase subfamily, although beta-1,6 branching and beta-1,4 bonds specifically define where Lam16A hydrolyzes its substrates, like curdlan (beta-1,3-glucan), lichenin (beta-1,3-1,4-mixed linkage glucan), and laminarin (beta-1,6-branched-1,3-glucan).
238806 QPRTase 8.12e-120 22 297 1 268
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.
238802 QPRTase_NadC 3.21e-111 22 297 1 269
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.
272894 nadC 3.19e-110 24 298 1 265
nicotinate-nucleotide pyrophosphorylase. Synonym: quinolinate phosphoribosyltransferase (decarboxylating) [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]
223235 NadC 3.17e-97 16 300 1 279
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.19e-189 313 673 11 370
1.06e-142 307 681 1 373
5.68e-125 309 672 6 382
1.78e-85 307 673 1 318
1.20e-84 328 670 16 313

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.30e-103 15 298 5 292
Crystal structure at 1.9A of the apo quinolinate phosphoribosyl transferase (BNA6) from Saccharomyces cerevisiae [Saccharomyces cerevisiae],3C2F_A Crystal structure of the quinolinate phosphoribosyl transferase (BNA6) from Saccharomyces cerevisiae complexed with PRPP [Saccharomyces cerevisiae],3C2O_A Crystal structure of the quinolinate phosphoribosyl transferase (BNA6) from Sachharomyces cerevisiae complexed with quinolinate [Saccharomyces cerevisiae],3C2V_A Crystal structure of the quinolinate phosphoribosyl transferase (BNA6) from Saccharomyces cerevisiae complexed with PRPP and the inhibitor phthalate [Saccharomyces cerevisiae]
2.38e-103 15 298 6 293
Crystal structure of the quinolinate phosphoribosyl transferase (BNA6) from Sachharomyces cerevisiae complexed with the inhibitor phthalate [Saccharomyces cerevisiae],3C2R_B Crystal structure of the quinolinate phosphoribosyl transferase (BNA6) from Sachharomyces cerevisiae complexed with the inhibitor phthalate [Saccharomyces cerevisiae]
1.34e-88 9 301 5 290
Qprtase Structure From Human [Homo sapiens],2JBM_B Qprtase Structure From Human [Homo sapiens],2JBM_C Qprtase Structure From Human [Homo sapiens],2JBM_D Qprtase Structure From Human [Homo sapiens],2JBM_E Qprtase Structure From Human [Homo sapiens],2JBM_F Qprtase Structure From Human [Homo sapiens],2JBM_G Qprtase Structure From Human [Homo sapiens],2JBM_H Qprtase Structure From Human [Homo sapiens],2JBM_I Qprtase Structure From Human [Homo sapiens],2JBM_J Qprtase Structure From Human [Homo sapiens],2JBM_K Qprtase Structure From Human [Homo sapiens],2JBM_L Qprtase Structure From Human [Homo sapiens]
1.63e-88 9 301 3 288
CRYSTAL STRUCTURE OF HUMAN QUINOLINATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH THE REACTANT QUINOLINATE [Homo sapiens],5AYY_B CRYSTAL STRUCTURE OF HUMAN QUINOLINATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH THE REACTANT QUINOLINATE [Homo sapiens],5AYY_C CRYSTAL STRUCTURE OF HUMAN QUINOLINATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH THE REACTANT QUINOLINATE [Homo sapiens],5AYY_D CRYSTAL STRUCTURE OF HUMAN QUINOLINATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH THE REACTANT QUINOLINATE [Homo sapiens],5AYY_E CRYSTAL STRUCTURE OF HUMAN QUINOLINATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH THE REACTANT QUINOLINATE [Homo sapiens],5AYY_F CRYSTAL STRUCTURE OF HUMAN QUINOLINATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH THE REACTANT QUINOLINATE [Homo sapiens],5AYY_G CRYSTAL STRUCTURE OF HUMAN QUINOLINATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH THE REACTANT QUINOLINATE [Homo sapiens],5AYY_H CRYSTAL STRUCTURE OF HUMAN QUINOLINATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH THE REACTANT QUINOLINATE [Homo sapiens],5AYY_I CRYSTAL STRUCTURE OF HUMAN QUINOLINATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH THE REACTANT QUINOLINATE [Homo sapiens],5AYZ_A Crystal Structure Of Human Quinolinate Phosphoribosyltransferase In Complex With The Product Nicotinate Mononucleotide [Homo sapiens],5AYZ_B Crystal Structure Of Human Quinolinate Phosphoribosyltransferase In Complex With The Product Nicotinate Mononucleotide [Homo sapiens],5AYZ_C Crystal Structure Of Human Quinolinate Phosphoribosyltransferase In Complex With The Product Nicotinate Mononucleotide [Homo sapiens],5AYZ_D Crystal Structure Of Human Quinolinate Phosphoribosyltransferase In Complex With The Product Nicotinate Mononucleotide [Homo sapiens],5AYZ_E Crystal Structure Of Human Quinolinate Phosphoribosyltransferase In Complex With The Product Nicotinate Mononucleotide [Homo sapiens],5AYZ_F Crystal Structure Of Human Quinolinate Phosphoribosyltransferase In Complex With The Product Nicotinate Mononucleotide [Homo sapiens],5AYZ_G Crystal Structure Of Human Quinolinate Phosphoribosyltransferase In Complex With The Product Nicotinate Mononucleotide [Homo sapiens],5AYZ_H Crystal Structure Of Human Quinolinate Phosphoribosyltransferase In Complex With The Product Nicotinate Mononucleotide [Homo sapiens],5AYZ_I Crystal Structure Of Human Quinolinate Phosphoribosyltransferase In Complex With The Product Nicotinate Mononucleotide [Homo sapiens],5AYZ_J Crystal Structure Of Human Quinolinate Phosphoribosyltransferase In Complex With The Product Nicotinate Mononucleotide [Homo sapiens],5AYZ_K Crystal Structure Of Human Quinolinate Phosphoribosyltransferase In Complex With The Product Nicotinate Mononucleotide [Homo sapiens],5AYZ_L Crystal Structure Of Human Quinolinate Phosphoribosyltransferase In Complex With The Product Nicotinate Mononucleotide [Homo sapiens]
5.57e-88 9 301 7 292
Crystal Structure of human apo-QPRT [Homo sapiens],4KWV_B Crystal Structure of human apo-QPRT [Homo sapiens],4KWV_C Crystal Structure of human apo-QPRT [Homo sapiens],4KWV_D Crystal Structure of human apo-QPRT [Homo sapiens],4KWV_E Crystal Structure of human apo-QPRT [Homo sapiens],4KWV_F Crystal Structure of human apo-QPRT [Homo sapiens],4KWW_A The crystal structure of human quinolinic acid phosphoribosyltransferase in complex with its inhibitor phthalic acid [Homo sapiens],4KWW_B The crystal structure of human quinolinic acid phosphoribosyltransferase in complex with its inhibitor phthalic acid [Homo sapiens],4KWW_C The crystal structure of human quinolinic acid phosphoribosyltransferase in complex with its inhibitor phthalic acid [Homo sapiens],4KWW_D The crystal structure of human quinolinic acid phosphoribosyltransferase in complex with its inhibitor phthalic acid [Homo sapiens],4KWW_E The crystal structure of human quinolinic acid phosphoribosyltransferase in complex with its inhibitor phthalic acid [Homo sapiens],4KWW_F The crystal structure of human quinolinic acid phosphoribosyltransferase in complex with its inhibitor phthalic acid [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.22e-102 15 298 6 293
Nicotinate-nucleotide pyrophosphorylase [carboxylating] OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=BNA6 PE=1 SV=1
1.79e-88 16 298 13 289
Nicotinate-nucleotide pyrophosphorylase [carboxylating] (Fragment) OS=Nematostella vectensis OX=45351 GN=qprt PE=3 SV=1
2.52e-87 9 301 3 288
Nicotinate-nucleotide pyrophosphorylase [carboxylating] OS=Homo sapiens OX=9606 GN=QPRT PE=1 SV=3
1.17e-85 13 298 3 297
Nicotinate-nucleotide pyrophosphorylase [carboxylating] OS=Dictyostelium discoideum OX=44689 GN=qprt PE=3 SV=1
2.23e-85 16 298 10 285
Nicotinate-nucleotide pyrophosphorylase [carboxylating] OS=Mus musculus OX=10090 GN=Qprt PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000053 0.000003

TMHMM  Annotations      help

There is no transmembrane helices in OAG24241.1.