| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G031065_T01 |
| Family | CE10 |
| Protein Properties | Length: 356 Molecular Weight: 37593 Isoelectric Point: 9.9123 |
| Chromosome | Chromosome/Scaffold: 1 Start: 199740743 End: 199742155 |
| Description | alpha/beta-Hydrolases superfamily protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| CE10 | 73 | 352 | 0 |
| PASVDPRTGVASRDVVVDHGTGLAVRLYRPSRQAVAGGAGGRLPVLVYFHGGAFVVESAFDPVYHGYLNALTAKAGVIAVSVNYRLAPEHPLPAAYEDAW AALAWVVANANANARRGGAGAGDPWLSRHGDASRLFLAGDSAGGNIAQNLAMRAAGQQQRIRGLALLDPYFLGRYVGGGAARAWDFICAGRYGMDHPYVD PMALPAEVLRRLPSPRVLMTVSEQDRLGPFQRAYVDALRGSGWRGRARLYVTPGEGHCYFLNNLASPKAAMHMATLAAFI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 356 Download |
| MASPVLLVAA LCSLFALLGA AGEPARGAAA EASALRSKAA TDPNTEVKFD FTPFLIQYKS 60 GRVHRFMGTS FVPASVDPRT GVASRDVVVD HGTGLAVRLY RPSRQAVAGG AGGRLPVLVY 120 FHGGAFVVES AFDPVYHGYL NALTAKAGVI AVSVNYRLAP EHPLPAAYED AWAALAWVVA 180 NANANARRGG AGAGDPWLSR HGDASRLFLA GDSAGGNIAQ NLAMRAAGQQ QRIRGLALLD 240 PYFLGRYVGG GAARAWDFIC AGRYGMDHPY VDPMALPAEV LRRLPSPRVL MTVSEQDRLG 300 PFQRAYVDAL RGSGWRGRAR LYVTPGEGHC YFLNNLASPK AAMHMATLAA FINGS* 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 6.0e-7 | 111 | 160 | 50 | + Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate. | ||
| COG2272 | PnbA | 7.0e-9 | 69 | 161 | 93 | + Carboxylesterase type B [Lipid metabolism] | ||
| pfam00135 | COesterase | 5.0e-10 | 112 | 160 | 49 | + Carboxylesterase family. | ||
| COG0657 | Aes | 2.0e-24 | 51 | 353 | 324 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 2.0e-32 | 118 | 333 | 239 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0008152 | metabolic process |
| GO:0016787 | hydrolase activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EAZ07335.1 | 0 | 13 | 353 | 5 | 330 | hypothetical protein OsI_29584 [Oryza sativa Indica Group] |
| GenBank | EAZ43068.1 | 0 | 13 | 353 | 5 | 330 | hypothetical protein OsJ_27658 [Oryza sativa Japonica Group] |
| RefSeq | NP_001062034.1 | 0 | 13 | 353 | 5 | 330 | Os08g0475100 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001152298.1 | 0 | 28 | 353 | 25 | 352 | gibberellin receptor GID1L2 [Zea mays] |
| RefSeq | XP_002444515.1 | 0 | 18 | 355 | 20 | 355 | hypothetical protein SORBIDRAFT_07g023110 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ed1_F | 1e-33 | 48 | 314 | 25 | 312 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum (Apo Form) |
| PDB | 3ed1_E | 1e-33 | 48 | 314 | 25 | 312 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum (Apo Form) |
| PDB | 3ed1_D | 1e-33 | 48 | 314 | 25 | 312 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum (Apo Form) |
| PDB | 3ed1_C | 1e-33 | 48 | 314 | 25 | 312 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum (Apo Form) |
| PDB | 3ed1_B | 1e-33 | 48 | 314 | 25 | 312 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum (Apo Form) |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| formononetin biosynthesis | RXN-3284 | EC-4.2.1.105 | 2-hydroxyisoflavanone dehydratase |
| isoflavonoid biosynthesis I | RXN-3284 | EC-4.2.1.105 | 2-hydroxyisoflavanone dehydratase |
| isoflavonoid biosynthesis II | RXN-3303 | EC-4.2.1.105 | 2-hydroxyisoflavanone dehydratase |
