Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma09g02630.1 |
Family | AA7 |
Protein Properties | Length: 534 Molecular Weight: 59544.1 Isoelectric Point: 10.2199 |
Chromosome | Chromosome/Scaffold: 09 Start: 1793414 End: 1795015 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 70 | 526 | 0 |
NARFNTSSTPKPLLIVTPLTESHVQAAVICAKTVNVQLKIRSGGHDYEGISYISKKHPFIVLDMFNLRKIKVDIKNEVAVVQAGAVMGEVYYRIWKKSKV HGFSAAVCPTVGVGGHISGGGYGNMLRKYGLSVDNVIDAQIVDVKGNLLNRKTMGEDLFWAIRGGGGASFGVIVSFTIKLLPVPKTVTVFRVERTLEQNA TDLVLQWQQVAPTTDPGLFLRLLLQPEGKTVTASVVALFLGGAKELVSILEKEFPLLGLKKESCTEMRWIDSVLWFYDDKSLKNGAKPETLLDRHVNTAF FLKRKSDYVQKAIPREGLECIFKRMIKLGKIGLVFNPYGGRMAEIPSDATPFPHRKGNLFKIQYSVNWFDPSVGAAKNFTNQAKKLYNYMTPFVSKNPRS AFLNYRDLDIGVNRFGKNSFQEGEVYGAKYFNNNFQRLVKVKTKVDPDNFFRNEQSI |
Full Sequence |
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Protein Sequence Length: 534 Download |
MVKPNSLAYL SATFLLLTVS TLVSAHSSLH HTFLQCLTHH TKNCSTQLSD IVFANTNPKF 60 PTVLQNYIRN ARFNTSSTPK PLLIVTPLTE SHVQAAVICA KTVNVQLKIR SGGHDYEGIS 120 YISKKHPFIV LDMFNLRKIK VDIKNEVAVV QAGAVMGEVY YRIWKKSKVH GFSAAVCPTV 180 GVGGHISGGG YGNMLRKYGL SVDNVIDAQI VDVKGNLLNR KTMGEDLFWA IRGGGGASFG 240 VIVSFTIKLL PVPKTVTVFR VERTLEQNAT DLVLQWQQVA PTTDPGLFLR LLLQPEGKTV 300 TASVVALFLG GAKELVSILE KEFPLLGLKK ESCTEMRWID SVLWFYDDKS LKNGAKPETL 360 LDRHVNTAFF LKRKSDYVQK AIPREGLECI FKRMIKLGKI GLVFNPYGGR MAEIPSDATP 420 FPHRKGNLFK IQYSVNWFDP SVGAAKNFTN QAKKLYNYMT PFVSKNPRSA FLNYRDLDIG 480 VNRFGKNSFQ EGEVYGAKYF NNNFQRLVKV KTKVDPDNFF RNEQSIPVCP SKA* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR00387 | glcD | 4.0e-5 | 129 | 258 | 141 | + glycolate oxidase, subunit GlcD. This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity [Energy metabolism, Other]. | ||
PRK11230 | PRK11230 | 3.0e-6 | 81 | 258 | 192 | + glycolate oxidase subunit GlcD; Provisional | ||
pfam08031 | BBE | 2.0e-16 | 470 | 527 | 58 | + Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine. | ||
pfam01565 | FAD_binding_4 | 8.0e-19 | 81 | 219 | 140 | + 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. | ||
COG0277 | GlcD | 2.0e-22 | 61 | 527 | 484 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
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 - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | NP_193816.1 | 0 | 29 | 533 | 34 | 539 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
RefSeq | XP_002299028.1 | 0 | 1 | 533 | 1 | 536 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317087.1 | 0 | 28 | 533 | 31 | 535 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523157.1 | 0 | 1 | 533 | 1 | 539 | Reticuline oxidase precursor, putative [Ricinus communis] |
RefSeq | XP_002523158.1 | 0 | 27 | 533 | 34 | 539 | Reticuline oxidase precursor, putative [Ricinus communis] |
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 | 4dns_B | 0 | 29 | 527 | 9 | 494 | 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_A | 0 | 29 | 527 | 9 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3tsj_B | 0 | 33 | 527 | 11 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3tsj_A | 0 | 33 | 527 | 11 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3tsh_A | 0 | 33 | 527 | 11 | 494 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cannabinoid biosynthesis | RXN-7854 | EC-1.21.3 | tetrahydrocannabinolic acid synthase |