Basic Information | |
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Species | Prunus persica |
Cazyme ID | ppa017360m |
Family | AA3 |
Protein Properties | Length: 532 Molecular Weight: 58551 Isoelectric Point: 6.1899 |
Chromosome | Chromosome/Scaffold: 1 Start: 7223301 End: 7225340 |
Description | Glucose-methanol-choline (GMC) oxidoreductase 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 |
AA3 | 44 | 532 | 0 |
QLEGTYDYIVVGGGTSGCSLAATLSEKYSVLVLERGTLPTAYPNLLTTDGFVYNLQQEDNGQTPVQRFVSEDGIDNVRGRVLGGTSMINAGVYARANISF YNQSGIEWDMDLVNKTYKWIEDTIVVRPNWQQWQALAGDGLFEAGVSPRNGFSLDHEPGIRLTGSTFDNNGTRHAADELLNNGDANNLRVGVHATVEKII FSNRNQLGKPAAVGVQYSDANLQSHQAFIHSKGEVILSAGTIGTPQLLLLSGVGPESYLSSLKIKVYHDNPYVGQYVYDNPRNFVNILPPKPLKPSYVTK LGITDDFYQCSISMSNYSTPPFSLFPSPSYPLPPSSFAHIVNKISGPLSYGYVTLRSSIDVRVAPNVKFNYFSNPIDLSHCVSGMKNIGDFLRTDSLKPY RANPDLPGIDGFNFLGIPLPKNQSDDASFKTFCQDAVASYWHYHGGCLVEKVVDDGLRVMGIDALRVVDATTFPSMPASHPQGFYMMLG |
Full Sequence |
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Protein Sequence Length: 532 Download |
MSVIVLVLHL FVLHLQYSEV HSLSNNHPHD FSYLKFVYNA SDPQLEGTYD YIVVGGGTSG 60 CSLAATLSEK YSVLVLERGT LPTAYPNLLT TDGFVYNLQQ EDNGQTPVQR FVSEDGIDNV 120 RGRVLGGTSM INAGVYARAN ISFYNQSGIE WDMDLVNKTY KWIEDTIVVR PNWQQWQALA 180 GDGLFEAGVS PRNGFSLDHE PGIRLTGSTF DNNGTRHAAD ELLNNGDANN LRVGVHATVE 240 KIIFSNRNQL GKPAAVGVQY SDANLQSHQA FIHSKGEVIL SAGTIGTPQL LLLSGVGPES 300 YLSSLKIKVY HDNPYVGQYV YDNPRNFVNI LPPKPLKPSY VTKLGITDDF YQCSISMSNY 360 STPPFSLFPS PSYPLPPSSF AHIVNKISGP LSYGYVTLRS SIDVRVAPNV KFNYFSNPID 420 LSHCVSGMKN IGDFLRTDSL KPYRANPDLP GIDGFNFLGI PLPKNQSDDA SFKTFCQDAV 480 ASYWHYHGGC LVEKVVDDGL RVMGIDALRV VDATTFPSMP ASHPQGFYMM LG 540 |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
pfam05199 | GMC_oxred_C | 2.0e-22 | 390 | 532 | 148 | + GMC oxidoreductase. This domain found associated with pfam00732. |
TIGR03970 | Rv0697 | 6.0e-29 | 50 | 532 | 527 | + dehydrogenase, Rv0697 family. This model describes a set of dehydrogenases belonging to the glucose-methanol-choline oxidoreductase (GMC oxidoreductase) family. Members of the present family are restricted to Actinobacterial genome contexts containing also members of families TIGR03962 and TIGR03969 (the mycofactocin system), and are proposed to be uniform in function. |
TIGR01810 | betA | 3.0e-32 | 50 | 517 | 545 | + choline dehydrogenase. Choline dehydrogenase catalyzes the conversion of exogenously supplied choline into the intermediate glycine betaine aldehyde, as part of a two-step oxidative reaction leading to the formation of osmoprotectant betaine. This enzymatic system can be found in both gram-positive and gram-negative bacteria. As in Escherichia coli , Staphylococcus xylosus , and Sinorhizobium meliloti, this enzyme is found associated in a transciptionally co-induced gene cluster with betaine aldehyde dehydrogenase, the second catalytic enzyme in this reaction. Other gram-positive organisms have been shown to employ a different enzymatic system, utlizing a soluable choline oxidase or type III alcohol dehydrogenase instead of choline dehydrogenase. This enzyme is a member of the GMC oxidoreductase family (pfam00732 and pfam05199), sharing a common evoluntionary origin and enzymatic reaction with alcohol dehydrogenase. Outgrouping from this model, Caulobacter crescentus shares sequence homology with choline dehydrogenase, yet other genes participating in this enzymatic reaction have not currently been identified [Cellular processes, Adaptations to atypical conditions]. |
COG2303 | BetA | 7.0e-46 | 46 | 532 | 544 | + Choline dehydrogenase and related flavoproteins [Amino acid transport and metabolism] |
PLN02785 | PLN02785 | 3.0e-144 | 32 | 532 | 537 | + Protein HOTHEAD |
Gene Ontology | |
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GO Term | Description |
GO:0016614 | oxidoreductase activity, acting on CH-OH group of donors |
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 |
GenBank | AAL11514.1 | 0 | 1 | 532 | 6 | 533 | AF412329_1 R-oxynitrile lyase isoenzyme 1 precursor [Prunus dulcis] |
DDBJ | BAH23314.1 | 0 | 16 | 532 | 22 | 535 | (R)-hydroxynitrile lyase [Prunus mume] |
Swiss-Prot | O50048 | 0 | 2 | 532 | 8 | 535 | MDL2_PRUSE RecName: Full=(R)-mandelonitrile lyase 2; AltName: Full=Hydroxynitrile lyase 2; Short=(R)-oxynitrilase 2; Flags: Precursor |
Swiss-Prot | P52706 | 0 | 1 | 532 | 6 | 533 | MDL1_PRUSE RecName: Full=(R)-mandelonitrile lyase 1; AltName: Full=Hydroxynitrile lyase 1; Short=(R)-oxynitrilase 1; Flags: Precursor |
Swiss-Prot | P52707 | 0 | 1 | 532 | 6 | 534 | MDL3_PRUSE RecName: Full=(R)-mandelonitrile lyase 3; AltName: Full=Hydroxynitrile lyase 3; Short=(R)-oxynitrilase 3; Flags: Precursor |
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 | 1ju2_B | 0 | 23 | 532 | 1 | 506 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
PDB | 1ju2_A | 0 | 23 | 532 | 1 | 506 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
PDB | 3gdp_B | 0 | 23 | 532 | 1 | 506 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
PDB | 3gdp_A | 0 | 23 | 532 | 1 | 506 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
PDB | 3gdn_B | 0 | 23 | 532 | 1 | 506 | A Chain A, Almond Hydroxynitrile Lyase In Complex With Benzaldehyde |