Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.089580.1 |
Family | AA3 |
Protein Properties | Length: 531 Molecular Weight: 57857.5 Isoelectric Point: 8.9458 |
Chromosome | Chromosome/Scaffold: 00894 Start: 988819 End: 990931 |
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 | 43 | 529 | 0 |
TDLPPKEEYDYIIIGGGTAGCPLATTLSSKFSVLLLERGSDPNKYPSVLNEQGLLNVFAAGDDGRNPFQRFVSEDGVENIRGRVLGGGSMVNAGFYSRGH REFFASAGVDWDMELVEKAYEWVEETVVSQPILNAWQSAFRSSLLEGGVVPDNGFDLRHLVGTKTGGSIFDNKGNRHGAVELLNKANPTNIKVAIEATVQ RILFSGLSANGVLYSDSKGKLHRAIIRKKGEIIVSAGAIGSPQLLLLSGIGPKSHLSSLKLPVVLHQPYVGQSMSDNPRFGTNIIIPFPVLPSSVKVVGI LQDNIYIQSIASPFPILIPQIFSLLPPQATSIIPTLAMFVGKFSEVHSEGSLRLNSSTNVKKSPIVGFNYYSHPDDLGRCVKGVRKMGDLLKTRTMEKIK TKNLEGNKGFEFLGVPLPENLWNDSSVEEYCKKTVTTYWHYHGGCLVGKVVDGNYKVIGIKNLRVVDGSTFSESPGTNPMATLMMLG |
Full Sequence |
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Protein Sequence Length: 531 Download |
MEHSRVTILI LSLMISIFQL QLHSSHAIPN QDVSYMKFVH NATDLPPKEE YDYIIIGGGT 60 AGCPLATTLS SKFSVLLLER GSDPNKYPSV LNEQGLLNVF AAGDDGRNPF QRFVSEDGVE 120 NIRGRVLGGG SMVNAGFYSR GHREFFASAG VDWDMELVEK AYEWVEETVV SQPILNAWQS 180 AFRSSLLEGG VVPDNGFDLR HLVGTKTGGS IFDNKGNRHG AVELLNKANP TNIKVAIEAT 240 VQRILFSGLS ANGVLYSDSK GKLHRAIIRK KGEIIVSAGA IGSPQLLLLS GIGPKSHLSS 300 LKLPVVLHQP YVGQSMSDNP RFGTNIIIPF PVLPSSVKVV GILQDNIYIQ SIASPFPILI 360 PQIFSLLPPQ ATSIIPTLAM FVGKFSEVHS EGSLRLNSST NVKKSPIVGF NYYSHPDDLG 420 RCVKGVRKMG DLLKTRTMEK IKTKNLEGNK GFEFLGVPLP ENLWNDSSVE EYCKKTVTTY 480 WHYHGGCLVG KVVDGNYKVI GIKNLRVVDG STFSESPGTN PMATLMMLGR * 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 | 8.0e-28 | 389 | 529 | 146 | + GMC oxidoreductase. This domain found associated with pfam00732. | ||
TIGR01810 | betA | 7.0e-33 | 52 | 529 | 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]. | ||
TIGR03970 | Rv0697 | 4.0e-40 | 52 | 529 | 520 | + 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. | ||
COG2303 | BetA | 3.0e-49 | 47 | 530 | 540 | + Choline dehydrogenase and related flavoproteins [Amino acid transport and metabolism] | ||
PLN02785 | PLN02785 | 2.0e-164 | 49 | 530 | 531 | + 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 | 1JU2 | 0 | 30 | 530 | 6 | 507 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
PDB | 3GDN | 0 | 30 | 530 | 6 | 507 | A Chain A, Almond Hydroxynitrile Lyase In Complex With Benzaldehyde |
GenBank | AAL11514.1 | 0 | 1 | 530 | 1 | 534 | AF412329_1 R-oxynitrile lyase isoenzyme 1 precursor [Prunus dulcis] |
Swiss-Prot | P52706 | 0 | 21 | 530 | 24 | 534 | MDL1_PRUSE RecName: Full=(R)-mandelonitrile lyase 1; AltName: Full=Hydroxynitrile lyase 1; Short=(R)-oxynitrilase 1; Flags: Precursor |
Swiss-Prot | P52707 | 0 | 1 | 530 | 1 | 535 | 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 | 3gdp_B | 0 | 30 | 530 | 6 | 507 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
PDB | 3gdp_A | 0 | 30 | 530 | 6 | 507 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
PDB | 3gdn_B | 0 | 30 | 530 | 6 | 507 | A Chain A, Almond Hydroxynitrile Lyase In Complex With Benzaldehyde |
PDB | 3gdn_A | 0 | 30 | 530 | 6 | 507 | A Chain A, Almond Hydroxynitrile Lyase In Complex With Benzaldehyde |
PDB | 1ju2_B | 0 | 30 | 530 | 6 | 507 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |