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Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna20173.1-v1.0-hybrid |
Family | AA7 |
Protein Properties | Length: 1464 Molecular Weight: 164508 Isoelectric Point: 9.9864 |
Chromosome | Chromosome/Scaffold: 3 Start: 8508917 End: 8517167 |
Description | FAD-binding Berberine family protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 74 | 286 | 0 |
TPSVPKPEFIFTPMLDSHVQAAVICAKELGIHLRVRSGGHDYEALSYVSQTETPFIIVDLAKLRSVNIDIEDNSAWVQAGASIGEVYYRIAEKSKTHGYP AGLCTSLGVGGHITGGAYGTMMRKYGLGADNVVDAHIVDASGRIHNRESMGEDLFWAIRGGGGASFGVILWWKIKLVPVPSTVTVFSVVKTLEQGATKLL HRYQQVAATELDE | |||
AA7 | 562 | 753 | 0 |
LGIHLRVRSGGHDYEGLSYVSQIETPFIIVDLAKLRSVNVDIRANSAWIQAGATIGEVYYRIAQKSRNHGFPAGLCTSLGVGGHITGGAYGTMMRKYGLA ADNVLDARIVDVNGRILNRKTMGEDLFWAIRGGGGASFGVILWWKIKLVPVPSTVTVFTVAKTLEQGATKLLHIWQQVAATKLDKDLNIRVL | |||
AA7 | 1029 | 1212 | 0 |
LGIHLRVRSGGHDYEGLSYVSQIETPFIVVDLSKLRSVNVDIQSNSAWIQAGATIGEVYYRIAEKSRTHGFPAGLYTSLGVGGHITGGAYGTMMRKYGLA ADNVLDARIVDVNGRILDRKTMGKDLFWAIRGGGGASFGVILWWKIKLVPVPSTVTVFSVSKTLEQGATKLLHRWQQVAATKLD |
Full Sequence |
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Protein Sequence Length: 1464 Download |
MMLPNPSIFS LFLFLLLSSA SWAHPKTSTL DSFSQCLSDN TEILIPFSKA FITPNNSTFL 60 PTLQSTAQNL RYLTPSVPKP EFIFTPMLDS HVQAAVICAK ELGIHLRVRS GGHDYEALSY 120 VSQTETPFII VDLAKLRSVN IDIEDNSAWV QAGASIGEVY YRIAEKSKTH GYPAGLCTSL 180 GVGGHITGGA YGTMMRKYGL GADNVVDAHI VDASGRIHNR ESMGEDLFWA IRGGGGASFG 240 VILWWKIKLV PVPSTVTVFS VVKTLEQGAT KLLHRYQQVA ATELDEDLFI RVIIQPTVFD 300 AKSGNKTIMT IYQAQFLGGV DRLLDVMGTS FPELGLTRKD CTQTSWLKSV MYIAGYPSNT 360 PPEVLLQGKS TFKNYFKAKS DFVKDPIPES ALEGIWKRLY EQASPLMIFN PYGGMMSKIS 420 ESEIPFPHRK GVLFKIQYLT TWQNGTEDEA EHMDWIRKLY NYMAPYVTMF PRQAYVNYRD 480 LDLGVNKKSN TSFIEASAWG NRYFKDNFNK LIKIKTKVDP DNFFRHEQSI PPLPLPLRTS 540 STTARQFSIH YRPKFNSTKP QLGIHLRVRS GGHDYEGLSY VSQIETPFII VDLAKLRSVN 600 VDIRANSAWI QAGATIGEVY YRIAQKSRNH GFPAGLCTSL GVGGHITGGA YGTMMRKYGL 660 AADNVLDARI VDVNGRILNR KTMGEDLFWA IRGGGGASFG VILWWKIKLV PVPSTVTVFT 720 VAKTLEQGAT KLLHIWQQVA ATKLDKDLNI RVLIQPTVLD SKSGKRTVTT LYQGQFLGGV 780 KRLLNVMQTG FPELNLTRKD CTQTSWLNSV MYIAGYATGT RPEVLLQGKP TFKNYFKSKS 840 DFVKDPIPET ALEGLWKRLL EETAPLIIWN PYGGMMSKIS ESAIPFPHRN VLFKIQYLTT 900 WQGANENEAK HINWIRKLYT YMAPYVTKSP RQAYVNYKDL DLGINKKKNT SIAEASAWGN 960 SALVADFSYE HVQTELRFIV PLEIAGKKPP PLYVTGFLWN LKTSKHYLFH FKQFCIHYHP 1020 KFNCTKPQLG IHLRVRSGGH DYEGLSYVSQ IETPFIVVDL SKLRSVNVDI QSNSAWIQAG 1080 ATIGEVYYRI AEKSRTHGFP AGLYTSLGVG GHITGGAYGT MMRKYGLAAD NVLDARIVDV 1140 NGRILDRKTM GKDLFWAIRG GGGASFGVIL WWKIKLVPVP STVTVFSVSK TLEQGATKLL 1200 HRWQQVAATK LDRHLNIRVL IQPTVVDSIS GKRTITTLFQ GQFLGGVKRL LNVMQTGFPE 1260 LNLTRKDCTE SNWLNSVMYI AGYANGTRPE VLLQGKPPFK SYFKAKSDFV KDPIPETALE 1320 GIWKRMLEET SSLIIWNPYG GVMSEISESA IPFPHRKVLF KIQYLTGWLA ANEDEAKHID 1380 WIRKLYSYMT PYVTKSPRQA YVNYRDLDLG INKKKNTSIA EASAWGTRYF KDNFYRLIKI 1440 KTKVDPHNFF RHEQSIPPLA RKA* 1500 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 2.0e-20 | 92 | 249 | 167 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
COG0277 | GlcD | 1.0e-20 | 1028 | 1176 | 156 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 3.0e-21 | 561 | 679 | 120 | + 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 oxidises 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. | ||
pfam01565 | FAD_binding_4 | 9.0e-23 | 1028 | 1146 | 120 | + 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 oxidises 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. | ||
pfam01565 | FAD_binding_4 | 2.0e-24 | 80 | 219 | 141 | + 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 oxidises 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. |
Gene Ontology | |
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GO Term | Description |
GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
GO:0016491 | oxidoreductase activity |
GO:0050660 | flavin adenine dinucleotide binding |
GO:0055114 | oxidation-reduction process |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3vte_A | 0 | 23 | 534 | 1 | 514 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3vte_A | 0 | 1024 | 1459 | 72 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3vte_A | 0 | 532 | 968 | 52 | 489 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 32 | 533 | 12 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 4dns_B | 0 | 1017 | 1459 | 66 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |