y
Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 98722 |
Family | AA7 |
Protein Properties | Length: 540 Molecular Weight: 58960.6 Isoelectric Point: 7.9713 |
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 | 70 | 257 | 5.1e-30 |
RRLPHAILYPSSVRDIASLVRAVHDTSSPLRIAARGAGHSVAGQAQAGDGVVIEMGSLRGIKVSEGKPGEQPYVEAMGGELWIDVVRESLKYGLAPRSLT DYLFLSVGGTLSNAGVSGQAFRYGPQISNVLELEVVTGNGEIVRCSPVDHADLFFAVLGGLGQFGIITKAKINLERAPQKVKWIRALY |
Full Sequence |
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Protein Sequence Length: 540 Download |
MLILSWGQIL ALLLLFVRTA IVGLANSSCS GSPLSAQDCA ALSSLSLHGH ITFATATSPA 60 SSSDFGRIHR RLPHAILYPS SVRDIASLVR AVHDTSSPLR IAARGAGHSV AGQAQAGDGV 120 VIEMGSLRGI KVSEGKPGEQ PYVEAMGGEL WIDVVRESLK YGLAPRSLTD YLFLSVGGTL 180 SNAGVSGQAF RYGPQISNVL ELEVVTGNGE IVRCSPVDHA DLFFAVLGGL GQFGIITKAK 240 INLERAPQKV KWIRALYSDF KAFTRDQELL IARPKHSPNS FDYVEGSVIV NNNHPSNEYK 300 PIPFHGQTLN ASLIPPSAGP VLYCLELTKN YDEDESATID ETVSSLLAPL GHVPSLVFSK 360 DASYFEFLNR VHDGEIRLRK KGLWDVPHPW MNLLVPKSKI EEFDALVFRE ILRKGINGPL 420 LVYPLDKMKW DSRTSVVMPD ENIFYLVGML RYATPSGVPS VSSLVDQNKE ILRVCKSAGI 480 HLKQYIPQLS SEEEWREHYG SSWSLFLRRK LAYDPKAILA PGQNIFAPSS SSLKLSSAL* 540 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01679 | bact_FAD_ox | 4.0e-9 | 73 | 242 | 170 | + FAD-linked oxidoreductase. This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. | ||
pfam01565 | FAD_binding_4 | 5.0e-27 | 73 | 215 | 144 | + 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-30 | 66 | 525 | 472 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam09265 | Cytokin-bind | 4.0e-125 | 247 | 526 | 284 | + Cytokinin dehydrogenase 1, FAD and cytokinin binding. Members of this family adopt an alpha+beta sandwich structure with an antiparallel beta-sheet, in a ferredoxin-like fold. They are predominantly found in plant cytokinin dehydrogenase 1, where they are capable of binding both FAD and cytokinin substrates. The substrate displays a 'plug-into-socket' binding mode that seals the catalytic site and precisely positions the carbon atom undergoing oxidation in close contact with the reactive locus of the flavin. | ||
PLN02441 | PLN02441 | 0 | 5 | 528 | 527 | + cytokinin dehydrogenase |
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_001776926.1 | 0 | 31 | 535 | 18 | 522 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001777489.1 | 0 | 42 | 527 | 4 | 491 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001777510.1 | 0 | 37 | 533 | 56 | 551 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001784400.1 | 0 | 42 | 526 | 1 | 478 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001786014.1 | 0 | 57 | 533 | 6 | 487 | predicted protein [Physcomitrella patens subsp. patens] |
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 | 2q4w_A | 0 | 44 | 529 | 33 | 523 | A Chain A, Raphanus Sativus Anionic Peroxidase. |
PDB | 2exr_A | 0 | 44 | 529 | 33 | 523 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
PDB | 1w1s_A | 0 | 10 | 526 | 1 | 533 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
PDB | 1w1r_A | 0 | 10 | 526 | 1 | 533 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
PDB | 1w1q_A | 0 | 10 | 526 | 1 | 533 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cytokinins degradation | RXN-4621 | EC-1.5.99 | isopentenyladenine:FAD oxidoreductase |