y
Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.089610.1 |
Family | AA3 |
Protein Properties | Length: 531 Molecular Weight: 57707 Isoelectric Point: 7.2328 |
Chromosome | Chromosome/Scaffold: 00894 Start: 1023399 End: 1026212 |
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 | 32 | 529 | 0 |
MKFVQDASEFPIKEEYDYIIVGGGTTGCPLAATLSKKFSVLLIERGSEPSKYPSVLNEQQLLNVFTVEDDGKNPFNRFISEDGVENIRGRVLGGSSMING GVYSRADPEFFRTQLGMQELDMEMVEKAYEWVEEAIVFKPSLNLWQGAFRRFLVEGGVEPDNGFDLRDDVGTKISGSIFDENGTRHGAVELLNKAQPTNL KVAVQAIVQRILFSGLSANGVLYSDSKGKLHTAYIRKEGEIIVSAGAIGSPQLLLLSGIGPKSYLSSLQLPVVLHQPHVGQSMMDYPRFGYVLAWPFPLS FTSSKVIGISQNKTFYFQSIASTTPLSIPPLFSIFPPNSTSLTTTSLATIGGKFSKVASTGSLRLNSSADAASNPIVRFNYYSHPADVAMCVKGVRKVGG FLKTQTVENIKTRDLEGNKTIQFVGLPLPGNLSDDSAVGEFCKKTVTSYWHYHGGCLVGKVVDGNYSVIGVKNLRVLDGSTFAVSPGSNPTATLMMLA |
Full Sequence |
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Protein Sequence Length: 531 Download |
MENYSTMVAF LLLILVFLSH SQLGLNQDVS YMKFVQDASE FPIKEEYDYI IVGGGTTGCP 60 LAATLSKKFS VLLIERGSEP SKYPSVLNEQ QLLNVFTVED DGKNPFNRFI SEDGVENIRG 120 RVLGGSSMIN GGVYSRADPE FFRTQLGMQE LDMEMVEKAY EWVEEAIVFK PSLNLWQGAF 180 RRFLVEGGVE PDNGFDLRDD VGTKISGSIF DENGTRHGAV ELLNKAQPTN LKVAVQAIVQ 240 RILFSGLSAN GVLYSDSKGK LHTAYIRKEG EIIVSAGAIG SPQLLLLSGI GPKSYLSSLQ 300 LPVVLHQPHV GQSMMDYPRF GYVLAWPFPL SFTSSKVIGI SQNKTFYFQS IASTTPLSIP 360 PLFSIFPPNS TSLTTTSLAT IGGKFSKVAS TGSLRLNSSA DAASNPIVRF NYYSHPADVA 420 MCVKGVRKVG GFLKTQTVEN IKTRDLEGNK TIQFVGLPLP GNLSDDSAVG EFCKKTVTSY 480 WHYHGGCLVG KVVDGNYSVI GVKNLRVLDG STFAVSPGSN PTATLMMLAR * 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK02106 | PRK02106 | 6.0e-33 | 45 | 316 | 324 | + choline dehydrogenase; Validated | ||
TIGR03970 | Rv0697 | 2.0e-37 | 48 | 529 | 519 | + 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-38 | 48 | 529 | 550 | + 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 | 4.0e-52 | 43 | 530 | 546 | + Choline dehydrogenase and related flavoproteins [Amino acid transport and metabolism] | ||
PLN02785 | PLN02785 | 9.0e-138 | 8 | 530 | 581 | + 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 |
PDB | 3GDN | 0 | 26 | 530 | 6 | 507 | A Chain A, Almond Hydroxynitrile Lyase In Complex With Benzaldehyde |
GenBank | AAL11514.1 | 0 | 5 | 530 | 4 | 534 | AF412329_1 R-oxynitrile lyase isoenzyme 1 precursor [Prunus dulcis] |
Swiss-Prot | P52706 | 0 | 26 | 530 | 33 | 534 | MDL1_PRUSE RecName: Full=(R)-mandelonitrile lyase 1; AltName: Full=Hydroxynitrile lyase 1; Short=(R)-oxynitrilase 1; Flags: Precursor |
Swiss-Prot | P52707 | 0 | 5 | 530 | 4 | 535 | MDL3_PRUSE RecName: Full=(R)-mandelonitrile lyase 3; AltName: Full=Hydroxynitrile lyase 3; Short=(R)-oxynitrilase 3; Flags: Precursor |
RefSeq | XP_002311915.1 | 0 | 28 | 530 | 1 | 507 | predicted protein [Populus trichocarpa] |
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 | 3red_L | 0 | 26 | 530 | 6 | 508 | A Chain A, 3.0 A Structure Of The Prunus Mume Hydroxynitrile Lyase Isozyme-1 |
PDB | 3red_K | 0 | 26 | 530 | 6 | 508 | A Chain A, 3.0 A Structure Of The Prunus Mume Hydroxynitrile Lyase Isozyme-1 |
PDB | 3red_J | 0 | 26 | 530 | 6 | 508 | A Chain A, 3.0 A Structure Of The Prunus Mume Hydroxynitrile Lyase Isozyme-1 |
PDB | 3red_I | 0 | 26 | 530 | 6 | 508 | A Chain A, 3.0 A Structure Of The Prunus Mume Hydroxynitrile Lyase Isozyme-1 |
PDB | 3red_H | 0 | 26 | 530 | 6 | 508 | A Chain A, 3.0 A Structure Of The Prunus Mume Hydroxynitrile Lyase Isozyme-1 |