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CAZyme Information: P170DRAFT_393025-t37_1-p1

You are here: Home > Sequence: P170DRAFT_393025-t37_1-p1

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 Aspergillus steynii
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
CAZyme ID P170DRAFT_393025-t37_1-p1
CAZy Family GH13
CAZyme Description FAD binding domain protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
447 MSFO01000009|CGC9 50364.06 6.1893
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AsteyniiIBT23096 13430 1392250 235 13195
Gene Location Start: 1468724; End:1470194  Strand: +

Full Sequence      Download help

MQIIWRDNAD  AQVYETARLD  NVFNKHSPNR  FPLAIVKVTS  ENDVIAAVQL  AIQHKCQVSV60
RAGGHSFPVW  SVQDDSILVD  MGDWKQVKID  PEKSAATVTP  SVTSKELNDR  LALHGLMFPG120
GHCGDVGLGG  FLLQGGMGWN  CGNWGWGCEF  VEAVDVVTAQ  GQLVHCSAQQ  NEDLFWASRG180
AGPAFPGLIT  QFHVRLIPLP  LEIHSSMYIY  PQNLYYEAFN  WALALAPTLD  GDTEITAKAK240
CDEGKPVFAI  YFTSMKDTEA  DARAALQHVQ  NSRPAGALTE  SFCYKDSLGK  LYEVMSTLHP300
KNHRYLSDNV  YLKNDADVPG  LLEKACFTLP  HQKSYLFWTS  MRPWSRKKLP  EMALSMRSDH360
YFAVYLIWEK  EEDDRRCREW  LQQVMKKVEV  ESVGSYIGDS  DFELRLTEYW  TVDNAQRLTK420
IRDERDPDGR  INGGFPAASK  RSVSRQG447

Enzyme Prediction      help

EC 1.1.3.-:1

CAZyme Signature Domains help

Created with Snap224467891111341561782012232452682903123353573794024243451AA7
Family Start End Evalue family coverage
AA7 20 430 2.6e-73 0.9781659388646288

CDD Domains      download full data without filtering help

Created with Snap2244678911113415617820122324526829031233535737940242432167FAD_binding_432435GlcD32198FAD_lactone_ox155200PLN02441
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396238 FAD_binding_4 4.29e-25 32 167 1 139
FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
223354 GlcD 8.58e-25 32 435 32 454
FAD/FMN-containing dehydrogenase [Energy production and conversion].
273751 FAD_lactone_ox 8.04e-05 32 198 15 180
sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
215242 PLN02441 0.002 155 200 198 242
cytokinin dehydrogenase

CAZyme Hits      help

Created with Snap2244678911113415617820122324526829031233535737940242432208QUC19098.1|AA732208UNI23960.1|AA719203BAI44126.1|AA7|CBM1832203QBZ61916.1|AA7|CBM1832200AHG26149.1|AA7
Hit ID E-Value Query Start Query End Hit Start Hit End
QUC19098.1|AA7 1.03e-22 32 208 48 226
UNI23960.1|AA7 4.13e-20 32 208 48 226
BAI44126.1|AA7|CBM18 1.89e-19 19 203 263 447
QBZ61916.1|AA7|CBM18 2.52e-19 32 203 275 447
AHG26149.1|AA7 4.86e-19 32 200 42 213

PDB Hits      download full data without filtering help

Created with Snap2244678911113415617820122324526829031233535737940242424396FYD_A24396FYG_A24396FYF_A24394XLO_A24396FYB_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
6FYD_A 4.55e-24 2 439 21 463
The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
6FYG_A 1.12e-23 2 439 21 463
The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]
6FYF_A 1.12e-23 2 439 21 463
The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_B The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_C The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_D The crystal structure of EncM V135M mutant [Streptomyces maritimus]
4XLO_A 1.52e-23 2 439 21 463
Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_B Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_C Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_D Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],6FOQ_A The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_B The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_C The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_D The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOW_A The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_B The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_C The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_D The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FP3_A The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_B The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_C The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_D The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FY8_A The crystal structure of EncM bromide soak [Streptomyces maritimus],6FY9_A The crystal structure of EncM complex with xenon under 15 bars Xe pressure [Streptomyces maritimus],6FYA_A The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus],6FYA_B The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus]
6FYB_A 1.52e-23 2 439 21 463
The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus]

Swiss-Prot Hits      download full data without filtering help

Created with Snap224467891111341561782012232452682903123353573794024241433sp|A0A0E3D8N0|JANO_PENJA4431sp|A0A0E3D8N6|PENO_PENCR4431sp|A0A140JWT7|PTMO_PENSI1433sp|A0A2I6PJ02|NODO_HYPPI14235sp|A5ABH0|PYNB_ASPNC
Hit ID E-Value Query Start Query End Hit Start Hit End Description
sp|A0A0E3D8N0|JANO_PENJA 2.54e-98 1 433 6 441
FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
sp|A0A0E3D8N6|PENO_PENCR 2.55e-92 4 431 12 437
FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|A0A140JWT7|PTMO_PENSI 5.64e-91 4 431 12 437
FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|A0A2I6PJ02|NODO_HYPPI 6.36e-86 1 433 9 442
FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
sp|A5ABH0|PYNB_ASPNC 2.93e-22 14 235 60 282
FAD-linked oxidoreductase pynB OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=pynB PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000061 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in P170DRAFT_393025-t37_1-p1.