Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10033390 |
Family | AA3 |
Protein Properties | Length: 473 Molecular Weight: 52265.4 Isoelectric Point: 7.2968 |
Chromosome | Chromosome/Scaffold: 488 Start: 1088305 End: 1089818 |
Description | Glucose-methanol-choline (GMC) oxidoreductase family protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA3 | 24 | 463 | 0 |
ISEDGVPNARGRILGGSSTINAGFYSRADPGFYRDSGANWDLRMVNESYDWVERAVVFRPELRNWQSAVRDGLLEAGVDPYNGFTVDHVAGTKIGGSTFD GRGRRHSAADLLNYANASNIQVGVYASVERILLAYKGRRSSKTAVSAIGVVYRDRMGQYHHAMVRENGEVMLSAGAIGSPQLLLLSGIGPRPYLSYWGIP VMYHLPYVGQYLYDNPRNGISFVPAMPLEHSLIQVVGITELGAYVEAASNVIPFTLSPAHSIFVRAPSTPMYLTVATLMEKIIGPQSVGYLRLASTDVRV NPIVRFNYFSSPVDMERCVNGTRKIGDVLRSRAMAEFMFREWYGGRNFRFVGPALPVDQSDYEQMADFCRRTVSTIWHYHGGCVVGKVVDEDFRVLGIQS LRIVDGSTFTISPGTNPQATLMMLGRYVGLKLIKEREEVF |
Full Sequence |
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Protein Sequence Length: 473 Download |
MTQEGFLSTL TNVDSFDSAA QSFISEDGVP NARGRILGGS STINAGFYSR ADPGFYRDSG 60 ANWDLRMVNE SYDWVERAVV FRPELRNWQS AVRDGLLEAG VDPYNGFTVD HVAGTKIGGS 120 TFDGRGRRHS AADLLNYANA SNIQVGVYAS VERILLAYKG RRSSKTAVSA IGVVYRDRMG 180 QYHHAMVREN GEVMLSAGAI GSPQLLLLSG IGPRPYLSYW GIPVMYHLPY VGQYLYDNPR 240 NGISFVPAMP LEHSLIQVVG ITELGAYVEA ASNVIPFTLS PAHSIFVRAP STPMYLTVAT 300 LMEKIIGPQS VGYLRLASTD VRVNPIVRFN YFSSPVDMER CVNGTRKIGD VLRSRAMAEF 360 MFREWYGGRN FRFVGPALPV DQSDYEQMAD FCRRTVSTIW HYHGGCVVGK VVDEDFRVLG 420 IQSLRIVDGS TFTISPGTNP QATLMMLGRY VGLKLIKERE EVFEMKSETG DL* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01810 | betA | 1.0e-29 | 16 | 448 | 491 | + 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]. | ||
pfam05199 | GMC_oxred_C | 8.0e-31 | 308 | 448 | 146 | + GMC oxidoreductase. This domain found associated with pfam00732. | ||
TIGR03970 | Rv0697 | 1.0e-31 | 32 | 448 | 446 | + 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 | 5.0e-35 | 32 | 449 | 474 | + Choline dehydrogenase and related flavoproteins [Amino acid transport and metabolism] | ||
PLN02785 | PLN02785 | 9.0e-166 | 4 | 459 | 498 | + 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 | ABE65766.1 | 0 | 1 | 459 | 94 | 550 | mandelonitrile lyase [Arabidopsis thaliana] |
GenBank | ACN31582.1 | 0 | 2 | 461 | 96 | 584 | unknown [Zea mays] |
RefSeq | NP_177448.1 | 0 | 1 | 459 | 94 | 550 | (R)-mandelonitrile lyase, putative / (R)-oxynitrilase, putative [Arabidopsis thaliana] |
RefSeq | XP_002277531.1 | 0 | 1 | 459 | 90 | 546 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002311915.1 | 0 | 1 | 459 | 60 | 517 | 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 | 3gdp_B | 0 | 1 | 459 | 67 | 517 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
PDB | 3gdp_A | 0 | 1 | 459 | 67 | 517 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
PDB | 3gdn_B | 0 | 1 | 459 | 67 | 517 | A Chain A, Almond Hydroxynitrile Lyase In Complex With Benzaldehyde |
PDB | 3gdn_A | 0 | 1 | 459 | 67 | 517 | A Chain A, Almond Hydroxynitrile Lyase In Complex With Benzaldehyde |
PDB | 1ju2_B | 0 | 1 | 459 | 67 | 517 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO796743 | 491 | 4 | 459 | 0 |
GO514057 | 227 | 179 | 405 | 0 |
FD579520 | 251 | 182 | 432 | 0 |
FS465759 | 245 | 197 | 440 | 0 |
FD583494 | 192 | 268 | 459 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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