Basic Information | |
---|---|
Species | Picea abies |
Cazyme ID | MA_228933g0010 |
Family | AA7 |
Protein Properties | Length: 544 Molecular Weight: 59810.7 Isoelectric Point: 6.7795 |
View CDS |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
AA7 | 72 | 287 | 0 |
GVAKPGVIAIPQSREEVRTGVVCCVQHGWEIRVRSGGHSYEGLSYISDVPFVLIDLMNLDKVDVDTESMTAWVEGGATLGQVYSGIAEKTETHGFPGGIC HTVGSGGHIAGGGQGFLSRKYGLAADNVIDALLVNASGNIMNKKTMGDHVFWALRGGGGGSWGVVIAIKLVSVPSILTAFNVSRTGRDAVTEAVRRWQSV GPTMDDDMFVRVQLFG |
Full Sequence |
---|
Protein Sequence Length: 544 Download |
MGKCCITPCF SILLALFMAF TTAGSVSDGP DPVKLISCLK VRGLTNITTS SSTQYDDLLY 60 FSAQNLRFAK PGVAKPGVIA IPQSREEVRT GVVCCVQHGW EIRVRSGGHS YEGLSYISDV 120 PFVLIDLMNL DKVDVDTESM TAWVEGGATL GQVYSGIAEK TETHGFPGGI CHTVGSGGHI 180 AGGGQGFLSR KYGLAADNVI DALLVNASGN IMNKKTMGDH VFWALRGGGG GSWGVVIAIK 240 LVSVPSILTA FNVSRTGRDA VTEAVRRWQS VGPTMDDDMF VRVQLFGINK VEGEKKTDVN 300 ASFQGMYLGG KDHLLLKMKK IFPELALVED DCHEMTWIES TAFFGETIKS VTELPDRYNS 360 QKTSFKIKSD IARTPLSTEA LHGLFERLEK QPLRAYALFS PLGGKMDDID SCALPFPYRA 420 GNIFDIQYNV LWNNEDEEPY IQWMGELYGY MASYVSSSPR AAYVNYLDLL MSLLRPGLLT 480 SIIWISIWAV QRMELPPSKT PPISGVKSIS WTISIDLSRP KRRWIATTIS ETLRAFPQSI 540 DRLS |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01678 | FAD_lactone_ox | 0.0003 | 65 | 286 | 228 | + sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include 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. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1. | ||
PLN02805 | PLN02805 | 3.0e-5 | 32 | 299 | 296 | + D-lactate dehydrogenase [cytochrome] | ||
COG0277 | GlcD | 2.0e-19 | 76 | 455 | 393 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 2.0e-21 | 76 | 211 | 137 | + 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. |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002264336.1 | 0 | 12 | 475 | 11 | 482 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299021.1 | 0 | 35 | 469 | 33 | 478 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002299025.1 | 0 | 47 | 469 | 3 | 432 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317084.1 | 0 | 5 | 488 | 7 | 480 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002332196.1 | 0 | 47 | 491 | 40 | 493 | predicted protein [Populus trichocarpa] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3vte_A | 0 | 53 | 469 | 27 | 460 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3d2j_A | 0 | 7 | 469 | 5 | 462 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3d2h_A | 0 | 7 | 469 | 5 | 462 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3d2d_A | 0 | 7 | 469 | 5 | 462 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
PDB | 3fw9_A | 0 | 35 | 469 | 2 | 437 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |