y
Basic Information | |
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Species | Zea mays |
Cazyme ID | GRMZM2G403076_T01 |
Family | AA7 |
Protein Properties | Length: 572 Molecular Weight: 62217.9 Isoelectric Point: 5.6715 |
Chromosome | Chromosome/Scaffold: 6 Start: 105434141 End: 105436791 |
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 | 96 | 336 | 0 |
PATVRPLWIVTPTNASHVQAAVACGRRHGVRLRVRSGGHDYEGLSYRSQRPEAFAVVDLSSLRAVRIDERSSTAWVDSGATLGELYYAVAQASGGRLAFP AGLCPTIGVGGHLSGGGFGTLLRKYGLASDNVLDAVLVDARGRLLDRAGMGSDVFWAIRGGGGESFGVVLSWQVRLVPVPPTVTAFRIPVAAGDGAALDV VARWQEVAPALPEDLFIRALLQNRSATFESLYLGTCDALVP |
Full Sequence |
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Protein Sequence Length: 572 Download |
MSQLLGFEIV YTWIELDDTT PQEAKMAIAR TRSSAPVLLL TFLCFYAIII PSNASPDDFP 60 QCLSGSIPSQ LVFAQSSPSF TSVLVSSIRN PRFFTPATVR PLWIVTPTNA SHVQAAVACG 120 RRHGVRLRVR SGGHDYEGLS YRSQRPEAFA VVDLSSLRAV RIDERSSTAW VDSGATLGEL 180 YYAVAQASGG RLAFPAGLCP TIGVGGHLSG GGFGTLLRKY GLASDNVLDA VLVDARGRLL 240 DRAGMGSDVF WAIRGGGGES FGVVLSWQVR LVPVPPTVTA FRIPVAAGDG AALDVVARWQ 300 EVAPALPEDL FIRALLQNRS ATFESLYLGT CDALVPVMGR RFPELGMNRT HCREMSWIET 360 VPYFFLGSGA TVEDILNRTT SLSTYAKMTS DYVRQAIPRR AWDGIFGKLA QPSAGLMILD 420 PYGAQVGAVP EPATPFPHRA GVLYNIQYVS VWSAGGDGAA HIEWVRDLYA FMEPHVSSNP 480 REAYFNYRDL DLGENVVGVD NISSYEAGKV WGEKYFVDNY ERLAVAKAEI DPDDYFRNEQ 540 SIPPLVPGSI ILPFSHVLCL ADMSSIVCSN LP 600 |
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 | 483 | 543 | 61 | + 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 | 5.0e-19 | 94 | 545 | 471 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 1.0e-20 | 101 | 241 | 142 | + 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 |
DDBJ | BAD53702.1 | 0 | 31 | 549 | 5 | 523 | putative CPRD2 [Oryza sativa Japonica Group] |
GenBank | EAZ01292.1 | 0 | 31 | 549 | 5 | 523 | hypothetical protein OsI_23321 [Oryza sativa Indica Group] |
RefSeq | NP_001057833.1 | 0 | 22 | 549 | 2 | 528 | Os06g0549900 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002438542.1 | 0 | 26 | 549 | 1 | 526 | hypothetical protein SORBIDRAFT_10g021690 [Sorghum bicolor] |
RefSeq | XP_002438543.1 | 0 | 26 | 545 | 1 | 525 | hypothetical protein SORBIDRAFT_10g021700 [Sorghum bicolor] |
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 | 58 | 546 | 12 | 497 | 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 | 58 | 546 | 12 | 497 | 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 | 50 | 546 | 2 | 497 | 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 | 50 | 546 | 2 | 497 | 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 | 50 | 546 | 2 | 497 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |