| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb07g003940.1 |
| Family | AA7 |
| Protein Properties | Length: 548 Molecular Weight: 58065.9 Isoelectric Point: 8.0631 |
| Chromosome | Chromosome/Scaffold: 7 Start: 4851881 End: 4854019 |
| 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 | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 80 | 471 | 0 |
| PSVGKPAAVVLPATKRDIQHAVLCARSTSLAIRVRSGGHSYEGLSYTTENHVPFMVIDLANLNHVDVDPVSATAWVESGATLGEVYHAVGLSNRTLAFSA GSCATVGMGGHAAGGGFGLLSRKFGLSADNVLDAVLIDASGDALTRATMPDDVFWAIRGGGGGSWGVVYAWKVRLVPVPDNITVFTVRRTGPAELIAGLM HRWQYVAPSLPDEFYLSAYIPTGPSSNGNHSISFTGQVLRPKRLAMSVLCQTFPELGLAESELSEVSWLESAVKFAGLSTVANLTSRQPGVGQYSKSKSD YVQAPISKQDAVKILRFMATAGSPAPEGAIQLDPYGGAMARIGSTMTPFPHRAGYLYSIQYSVSWKASDVDCADEYVGWLRSFYDFMAPYVT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 548 Download |
| MTTMNTMVAA AALALHLFAV SATRASTTQS SSPPPQPPAS AVDISSCLLS NGVANFSLPS 60 SPSYTPLLNS SIRNLRFALP SVGKPAAVVL PATKRDIQHA VLCARSTSLA IRVRSGGHSY 120 EGLSYTTENH VPFMVIDLAN LNHVDVDPVS ATAWVESGAT LGEVYHAVGL SNRTLAFSAG 180 SCATVGMGGH AAGGGFGLLS RKFGLSADNV LDAVLIDASG DALTRATMPD DVFWAIRGGG 240 GGSWGVVYAW KVRLVPVPDN ITVFTVRRTG PAELIAGLMH RWQYVAPSLP DEFYLSAYIP 300 TGPSSNGNHS ISFTGQVLRP KRLAMSVLCQ TFPELGLAES ELSEVSWLES AVKFAGLSTV 360 ANLTSRQPGV GQYSKSKSDY VQAPISKQDA VKILRFMATA GSPAPEGAIQ LDPYGGAMAR 420 IGSTMTPFPH RAGYLYSIQY SVSWKASDVD CADEYVGWLR SFYDFMAPYV TKNPRAAYVN 480 YLDLDLGTNG WMNATGGTSY GSVGHAASSW GQRYFLANFG SVLSFVVHTW MCLPRAFGYG 540 TSWPGCS* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01677 | pln_FAD_oxido | 0.006 | 86 | 178 | 95 | + plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown. | ||
| COG0277 | GlcD | 9.0e-19 | 83 | 294 | 222 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 2.0e-23 | 85 | 224 | 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 | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EAZ05659.1 | 0 | 26 | 524 | 15 | 508 | hypothetical protein OsI_27886 [Oryza sativa Indica Group] |
| RefSeq | NP_001061035.1 | 0 | 47 | 524 | 36 | 508 | Os08g0158200 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001140781.1 | 0 | 44 | 523 | 36 | 527 | hypothetical protein LOC100272856 [Zea mays] |
| RefSeq | XP_002445087.1 | 0 | 37 | 523 | 35 | 536 | hypothetical protein SORBIDRAFT_07g003930 [Sorghum bicolor] |
| RefSeq | XP_002445088.1 | 0 | 1 | 547 | 1 | 547 | hypothetical protein SORBIDRAFT_07g003940 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3fw9_A | 0 | 43 | 523 | 1 | 473 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 4ec3_A | 0 | 43 | 523 | 7 | 479 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
| PDB | 3gsy_A | 0 | 43 | 523 | 7 | 479 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| PDB | 3d2j_A | 0 | 43 | 523 | 26 | 498 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| PDB | 3d2h_A | 0 | 43 | 523 | 26 | 498 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| berberine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
| dehydroscoulerine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
| sanguinarine and macarpine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
