Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr4g005860.1 |
Family | AA3 |
Protein Properties | Length: 568 Molecular Weight: 61922.4 Isoelectric Point: 8.6204 |
Chromosome | Chromosome/Scaffold: 4 Start: 516291 End: 519451 |
Description | Glucose-methanol-choline (GMC) oxidoreductase family protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA3 | 45 | 562 | 0 |
ASEFPLEDYYDYIIVGGGTAGCPLAATLSQSHRVLILERGGVIHGKLNLMNQEGFLNTLLSATANNANNEDSPAQSFVSEDGVLNARGRVLGGSSAINAG FYSRADCEFFTKSGLNWDLKLVNESYEWVEREIVFRPDLKTWQSAVRDGLLEAGVGPYNGFTLDHATGTKIGGSTFDSQGKRHSSADLLRYARHSNLRIA VYASVERLLLASSSSSFAPNSATGSSVIGVLYRDQNGRYHHAMLKDFGEVILSAGAIGSPQLLLLSGIGPRPYLSSWGIPVAHHLPYVGHFLYDNPRNGI TILPSVPLEHSLIQVVGITNSGAYIEAASNVVPFLSPPQTAFIRSSASPLYLTVGTLISKISGPVSAGFLRLASTDVRFNPIVRFNYFSNGVDVEKCVNG TRKLGDVLRSRAMNDFKFRNWLGVRDFRFIGPALPNDQTDYAEMADFCKRTVSTIWHYHGGCVVGRVVNRHLKVIGIDSLRIVDGSVFSVSPGTNPQATL MMLGRYFGLKIIREREGK |
Full Sequence |
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Protein Sequence Length: 568 Download |
MEASSITVSL QFLLLLFFTT IFFPSSFASQ QQDKPPSYLK MVANASEFPL EDYYDYIIVG 60 GGTAGCPLAA TLSQSHRVLI LERGGVIHGK LNLMNQEGFL NTLLSATANN ANNEDSPAQS 120 FVSEDGVLNA RGRVLGGSSA INAGFYSRAD CEFFTKSGLN WDLKLVNESY EWVEREIVFR 180 PDLKTWQSAV RDGLLEAGVG PYNGFTLDHA TGTKIGGSTF DSQGKRHSSA DLLRYARHSN 240 LRIAVYASVE RLLLASSSSS FAPNSATGSS VIGVLYRDQN GRYHHAMLKD FGEVILSAGA 300 IGSPQLLLLS GIGPRPYLSS WGIPVAHHLP YVGHFLYDNP RNGITILPSV PLEHSLIQVV 360 GITNSGAYIE AASNVVPFLS PPQTAFIRSS ASPLYLTVGT LISKISGPVS AGFLRLASTD 420 VRFNPIVRFN YFSNGVDVEK CVNGTRKLGD VLRSRAMNDF KFRNWLGVRD FRFIGPALPN 480 DQTDYAEMAD FCKRTVSTIW HYHGGCVVGR VVNRHLKVIG IDSLRIVDGS VFSVSPGTNP 540 QATLMMLGRY FGLKIIRERE GKGTHEL* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK02106 | PRK02106 | 3.0e-31 | 272 | 548 | 325 | + choline dehydrogenase; Validated | ||
TIGR03970 | Rv0697 | 3.0e-32 | 55 | 548 | 540 | + 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 | 1.0e-34 | 55 | 560 | 563 | + 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 | 8.0e-40 | 54 | 559 | 569 | + Choline dehydrogenase and related flavoproteins [Amino acid transport and metabolism] | ||
PLN02785 | PLN02785 | 0 | 33 | 563 | 570 | + Protein HOTHEAD |
Gene Ontology | |
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GO Term | Description |
GO:0009055 | electron carrier activity |
GO:0016491 | oxidoreductase activity |
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 | 26 | 559 | 26 | 550 | mandelonitrile lyase [Arabidopsis thaliana] |
GenBank | ACN31582.1 | 0 | 24 | 562 | 20 | 585 | unknown [Zea mays] |
RefSeq | NP_177448.1 | 0 | 26 | 559 | 26 | 550 | (R)-mandelonitrile lyase, putative / (R)-oxynitrilase, putative [Arabidopsis thaliana] |
RefSeq | XP_002277531.1 | 0 | 3 | 559 | 2 | 546 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002311915.1 | 0 | 36 | 559 | 2 | 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 | 1ju2_B | 0 | 37 | 559 | 10 | 517 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
PDB | 1ju2_A | 0 | 37 | 559 | 10 | 517 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
PDB | 3gdp_B | 0 | 37 | 559 | 10 | 517 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
PDB | 3gdp_A | 0 | 37 | 559 | 10 | 517 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
PDB | 3gdn_B | 0 | 37 | 559 | 10 | 517 | A Chain A, Almond Hydroxynitrile Lyase In Complex With Benzaldehyde |