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CAZyme Information: OAG26150.1

You are here: Home > Sequence: OAG26150.1

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 OAG26150.1
CAZy Family GT45
CAZyme Description Carbamoyl-phosphate synthase (glutamine-hydrolyzing) [Source:UniProtKB/TrEMBL;Acc:A0A177E3Z5]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1240 133464.35 6.9569
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

EC 3.2.1.21:16 3.2.1.-:3

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH3 76 281 9.7e-58 0.9722222222222222

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223579 CarA 8.69e-173 805 1171 1 366
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism].
273580 CPSaseIIsmall 2.96e-165 808 1169 1 357
carbamoyl-phosphate synthase, small subunit. This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
237139 PRK12564 2.34e-161 814 1167 11 360
carbamoyl-phosphate synthase small subunit.
183784 PRK12838 6.69e-134 814 1169 9 352
carbamoyl phosphate synthase small subunit; Reviewed
153215 GATase1_CPSase 6.68e-99 987 1164 1 178
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 735 1 737
0.0 1 735 2 739
0.0 1 736 19 736
0.0 6 733 6 729
0.0 5 735 3 731

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.35e-312 34 736 9 711
Chain A, Beta-d-glucoside Glucohydrolase [Trichoderma reesei],3ZZ1_A Chain A, BETA-D-GLUCOSIDE GLUCOHYDROLASE [Trichoderma reesei]
3.47e-312 34 736 10 712
Chain A, Beta-D-glucoside glucohydrolase [Trichoderma reesei],4I8D_B Chain B, Beta-D-glucoside glucohydrolase [Trichoderma reesei]
3.06e-288 32 735 4 710
Crystasl Structure of Beta-glucosidase D2-BGL from Chaetomella Raphigera [Chaetomella raphigera]
6.37e-190 32 731 19 833
Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus [Aspergillus aculeatus],4IIB_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus [Aspergillus aculeatus],4IIC_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with isofagomine [Aspergillus aculeatus],4IIC_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with isofagomine [Aspergillus aculeatus],4IID_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with 1-deoxynojirimycin [Aspergillus aculeatus],4IID_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with 1-deoxynojirimycin [Aspergillus aculeatus],4IIE_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with calystegine B(2) [Aspergillus aculeatus],4IIE_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with calystegine B(2) [Aspergillus aculeatus],4IIF_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with castanospermine [Aspergillus aculeatus],4IIF_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with castanospermine [Aspergillus aculeatus],4IIG_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with D-glucose [Aspergillus aculeatus],4IIG_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with D-glucose [Aspergillus aculeatus],4IIH_A Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with thiocellobiose [Aspergillus aculeatus],4IIH_B Crystal structure of beta-glucosidase 1 from Aspergillus aculeatus in complex with thiocellobiose [Aspergillus aculeatus]
6.57e-190 32 735 20 838
Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus oryzae],5FJJ_B Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus oryzae],5FJJ_C Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus oryzae],5FJJ_D Three-dimensional structures of two heavily N-glycosylated Aspergillus sp. Family GH3 beta-D-glucosidases [Aspergillus oryzae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 30 736 20 724
Beta-glucosidase cel3A OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=cel3A PE=1 SV=1
2.06e-317 33 733 24 731
Probable beta-glucosidase L OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=bglL PE=3 SV=1
2.06e-317 33 733 24 731
Probable beta-glucosidase L OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=bglL PE=3 SV=1
1.64e-316 33 733 24 731
Probable beta-glucosidase L OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=bglL PE=3 SV=1
3.34e-315 29 736 20 735
Probable beta-glucosidase L OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=bglL PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000347 0.999632 CS pos: 29-30. Pr: 0.5875

TMHMM  Annotations      help

There is no transmembrane helices in OAG26150.1.