y
Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 112603 |
Family | AA3 |
Protein Properties | Length: 482 Molecular Weight: 51054 Isoelectric Point: 8.1767 |
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 | 7 | 479 | 0 |
QLKWNSYDYIIVGGGTAGCPLAATLSQRFKVLVLERGGFPDPISTRRDSFLLTYENQLGSNTLVQGFVSTDGVRNGRARVLGGGSSINAGFYNRASPQTI ADMGLDGSLANASFQWVERIVASFPELGPYQRAFRQSLLEAGVTPDNGASYDFQVGTQTGGTNFDSQGFRRPASNLFVYGNRTNLDVLLYAQVELILFKG LRAYGVRYTDFLGLPHTALLSRHPKSEVILCAGALGSPQLLLLSGIGPADHLTAMGIKVVLNATGVGQQMRDNPTTRLVILSPSPVESSLVQAVGITAAF GTYIEAASGAAAAAIPGAPVEYILQKAAGPLSVGKLVLGSTNVRDNPIVTFNYFQNPQDLATCVAGVNRVEEAVLTNAFRPFVFDIQPLPSGGTVGSPNR RNPAFAPTLNATIATYCVTNVATIWHYHGGCVVGQVVDSDYKVLGTQGLRVVDGSTFVFSPGTNPQATVMMLG |
Full Sequence |
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Protein Sequence Length: 482 Download |
MSEPSVQLKW NSYDYIIVGG GTAGCPLAAT LSQRFKVLVL ERGGFPDPIS TRRDSFLLTY 60 ENQLGSNTLV QGFVSTDGVR NGRARVLGGG SSINAGFYNR ASPQTIADMG LDGSLANASF 120 QWVERIVASF PELGPYQRAF RQSLLEAGVT PDNGASYDFQ VGTQTGGTNF DSQGFRRPAS 180 NLFVYGNRTN LDVLLYAQVE LILFKGLRAY GVRYTDFLGL PHTALLSRHP KSEVILCAGA 240 LGSPQLLLLS GIGPADHLTA MGIKVVLNAT GVGQQMRDNP TTRLVILSPS PVESSLVQAV 300 GITAAFGTYI EAASGAAAAA IPGAPVEYIL QKAAGPLSVG KLVLGSTNVR DNPIVTFNYF 360 QNPQDLATCV AGVNRVEEAV LTNAFRPFVF DIQPLPSGGT VGSPNRRNPA FAPTLNATIA 420 TYCVTNVATI WHYHGGCVVG QVVDSDYKVL GTQGLRVVDG STFVFSPGTN PQATVMMLGR 480 Y* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK02106 | PRK02106 | 2.0e-10 | 336 | 479 | 149 | + choline dehydrogenase; Validated | ||
TIGR01810 | betA | 5.0e-34 | 14 | 479 | 539 | + 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]. | ||
PRK02106 | PRK02106 | 2.0e-37 | 11 | 278 | 316 | + choline dehydrogenase; Validated | ||
COG2303 | BetA | 1.0e-45 | 11 | 480 | 548 | + Choline dehydrogenase and related flavoproteins [Amino acid transport and metabolism] | ||
PLN02785 | PLN02785 | 8.0e-164 | 11 | 481 | 522 | + Protein HOTHEAD |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI31862.1 | 0 | 13 | 481 | 47 | 528 | unnamed protein product [Vitis vinifera] |
EMBL | CBI34759.1 | 0 | 13 | 481 | 47 | 562 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002282510.1 | 0 | 13 | 481 | 13 | 528 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002298074.1 | 0 | 13 | 481 | 46 | 560 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002510860.1 | 0 | 13 | 481 | 46 | 561 | glucose-methanol-choline (gmc) oxidoreductase, putative [Ricinus communis] |
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 | 12 | 481 | 26 | 508 | A Chain A, Crystal Structure Of The Reconstituted Cota |
PDB | 3gdp_A | 0 | 12 | 481 | 26 | 508 | A Chain A, Crystal Structure Of The Reconstituted Cota |
PDB | 3gdn_B | 0 | 12 | 481 | 26 | 508 | A Chain A, Almond Hydroxynitrile Lyase In Complex With Benzaldehyde |
PDB | 3gdn_A | 0 | 12 | 481 | 26 | 508 | A Chain A, Almond Hydroxynitrile Lyase In Complex With Benzaldehyde |
PDB | 1ju2_B | 0 | 12 | 481 | 26 | 508 | A Chain A, Crystal Structure Of The Hydroxynitrile Lyase From Almond |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cutin biosynthesis | RXN-2121 | EC-1.1.1 | 18-hydroxyoleate dehydrogenase |
cutin biosynthesis | RXN-9802 | EC-1.1.1 | 16-hydroxypalmitate dehydrogenase |
suberin biosynthesis | RXN-2121 | EC-1.1.1 | 18-hydroxyoleate dehydrogenase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO796743 | 519 | 14 | 481 | 0 |
CK271873 | 308 | 11 | 311 | 0 |
CO080148 | 275 | 13 | 280 | 0 |
CO078158 | 246 | 71 | 311 | 0 |
EL438621 | 271 | 23 | 286 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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