Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma05g25540.1 |
Family | AA7 |
Protein Properties | Length: 583 Molecular Weight: 64452.9 Isoelectric Point: 6.9604 |
Chromosome | Chromosome/Scaffold: 05 Start: 31604682 End: 31608218 |
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 | 80 | 541 | 0 |
NARFNTTSTPKPLLVVTPSEDPHVQGAVICAKSIGIQLKIRSGGHDYEGISYVSDQPFIILDMFHFRNITVDVENEVAVVQAGATLGEVYYRIWEKSKVH GFPAGVCPTVGVGGHLSGGGYGNMLRKHGLSVDHVVDAKIVDVKGRILDKESMGEDLFWAIRGGGGASFGVILSYTVKLIPVPEVVTVFRIAKSLDQNES ATELVLQWQQVAPHTDHRLFMRLLLQPVSSKVVKGQRTIRATVMALFLGGADEVVTLMGKEFPALGLSKENCTELSWIDSVLWWSNFDNTTKPDALLDRD LNSASFLKRKSDYVQNPISKKGLEGIWEKMIELGKTGFVFNPYGGKMSEVSSDATPFPHRAGNLFKIQYSVNWDDPGVELEKNFTSQAKMLYSYMTPFVS SDPRSAFLNYRDLDIGTNSFGKNSYEEGAVYGVKYFNDNFKRLVKIKTEVDPENFFRNEQSI |
Full Sequence |
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Protein Sequence Length: 583 Download |
MVPTNPMEKS SLFPSGTFLF LLLVLLNVSA SVAAPTPESV YTSFLECLTN YTKAQDQVSN 60 IVFAQTNASF SSVLQAYIRN ARFNTTSTPK PLLVVTPSED PHVQGAVICA KSIGIQLKIR 120 SGGHDYEGIS YVSDQPFIIL DMFHFRNITV DVENEVAVVQ AGATLGEVYY RIWEKSKVHG 180 FPAGVCPTVG VGGHLSGGGY GNMLRKHGLS VDHVVDAKIV DVKGRILDKE SMGEDLFWAI 240 RGGGGASFGV ILSYTVKLIP VPEVVTVFRI AKSLDQNESA TELVLQWQQV APHTDHRLFM 300 RLLLQPVSSK VVKGQRTIRA TVMALFLGGA DEVVTLMGKE FPALGLSKEN CTELSWIDSV 360 LWWSNFDNTT KPDALLDRDL NSASFLKRKS DYVQNPISKK GLEGIWEKMI ELGKTGFVFN 420 PYGGKMSEVS SDATPFPHRA GNLFKIQYSV NWDDPGVELE KNFTSQAKML YSYMTPFVSS 480 DPRSAFLNYR DLDIGTNSFG KNSYEEGAVY GVKYFNDNFK RLVKIKTEVD PENFFRNEQS 540 IPIHPGPDTG AIKSGAGKLL HLTLYWSVMV KVGWLFILEL FI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK11230 | PRK11230 | 0.0003 | 91 | 280 | 200 | + glycolate oxidase subunit GlcD; Provisional | ||
TIGR00387 | glcD | 9.0e-5 | 138 | 267 | 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]. | ||
pfam08031 | BBE | 2.0e-16 | 485 | 542 | 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 | 3.0e-19 | 91 | 228 | 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 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 | 3.0e-20 | 72 | 302 | 242 | + 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 | XP_002270139.1 | 0 | 38 | 545 | 25 | 531 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299028.1 | 0 | 17 | 545 | 5 | 533 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317087.1 | 0 | 29 | 545 | 20 | 532 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523157.1 | 0 | 39 | 542 | 35 | 533 | Reticuline oxidase precursor, putative [Ricinus communis] |
RefSeq | XP_002523158.1 | 0 | 39 | 542 | 35 | 533 | 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 | 3vte_A | 0 | 43 | 545 | 6 | 514 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 34 | 542 | 1 | 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 | 34 | 542 | 1 | 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 | 37 | 542 | 4 | 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 | 37 | 542 | 4 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cannabinoid biosynthesis | RXN-7854 | EC-1.21.3 | tetrahydrocannabinolic acid synthase |