Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.010G221700.1 |
Family | AA7 |
Protein Properties | Length: 563 Molecular Weight: 62955 Isoelectric Point: 8.237 |
Chromosome | Chromosome/Scaffold: 10 Start: 59198974 End: 59201080 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 68 | 522 | 0 |
NARFNTSSTPKPLIIITPLDESHVSAAVICSQKLGFQVKIRSGGHDYEGLSYVFDKPFFVLDMFNLRSITVNMADETAWVGAGATLGELYYNIWKNSKVH GFPAGVCPTVGVGGHLSGAGYGTLIRKYGLSVDHVVDAKLVDVNGKILDRKTMGEDLFWAIRGGGAASFGVVLSYKIKLVPVPETVTVFRIERLLTENAT DITFKWQTIAPTTDENLFMRMLLQPVTRNKKKTARISVIALYLGDSDSLVSLLQKDFPELSIGKSNCNETTWIDSVLWWANFDLGTPPTALLDRDLNDAG FLKRKSDYVQTPIPKSGLESLWQKMIELGKVGMVFNAYGGRMDQIKPDETPFPHRAGNLYKIQYSVNWDQPGSEADKNFTTQAKLLHDFMTPFVSKNPRS AYFNYRDIDVGSTKKWSYEEGRVYGESYFNGNYERLVDVKTAVDANNFFRNEQSI |
Full Sequence |
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Protein Sequence Length: 563 Download |
MPNPMRPYLL LSVVFFFNLY HSMAVPDPTH QALLQCLTQS IPTDTASSII VSKSNPSYNS 60 VLRAYIRNAR FNTSSTPKPL IIITPLDESH VSAAVICSQK LGFQVKIRSG GHDYEGLSYV 120 FDKPFFVLDM FNLRSITVNM ADETAWVGAG ATLGELYYNI WKNSKVHGFP AGVCPTVGVG 180 GHLSGAGYGT LIRKYGLSVD HVVDAKLVDV NGKILDRKTM GEDLFWAIRG GGAASFGVVL 240 SYKIKLVPVP ETVTVFRIER LLTENATDIT FKWQTIAPTT DENLFMRMLL QPVTRNKKKT 300 ARISVIALYL GDSDSLVSLL QKDFPELSIG KSNCNETTWI DSVLWWANFD LGTPPTALLD 360 RDLNDAGFLK RKSDYVQTPI PKSGLESLWQ KMIELGKVGM VFNAYGGRMD QIKPDETPFP 420 HRAGNLYKIQ YSVNWDQPGS EADKNFTTQA KLLHDFMTPF VSKNPRSAYF NYRDIDVGST 480 KKWSYEEGRV YGESYFNGNY ERLVDVKTAV DANNFFRNEQ SIPPRSSSIL HSSYGSATCI 540 IIAVHTCWYY IVFIFSLCSD LF* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
pfam08031 | BBE | 2.0e-15 | 468 | 523 | 56 | + 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. |
COG0277 | GlcD | 1.0e-21 | 60 | 524 | 493 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
pfam01565 | FAD_binding_4 | 3.0e-26 | 79 | 216 | 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. |
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_002267223.1 | 0 | 27 | 524 | 32 | 530 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299028.1 | 0 | 6 | 523 | 3 | 530 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317087.1 | 0 | 27 | 527 | 30 | 535 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523157.1 | 0 | 30 | 527 | 37 | 537 | Reticuline oxidase precursor, putative [Ricinus communis] |
RefSeq | XP_002523158.1 | 0 | 30 | 527 | 37 | 537 | 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 | 33 | 524 | 13 | 495 | 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 | 33 | 524 | 13 | 495 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3vte_A | 0 | 31 | 524 | 5 | 512 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 26 | 524 | 4 | 495 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 26 | 524 | 4 | 495 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |