| Basic Information | |
|---|---|
| Species | Picea abies |
| Cazyme ID | MA_159144g0160 |
| Family | AA4 |
| Protein Properties | Length: 483 Molecular Weight: 51518.9 Isoelectric Point: 4.8192 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| AA4 | 18 | 204 | 4e-23 |
| ILDRRDAIVEHLARLVSSDGLITDRDECRAYETDAFAAYRKMPLAVVLPTSTNEVSAVLRFCHDNGVKVVPRGAGTSLAGGAIPTEDAIVLGLSRMSRVL EINYDDRFIRVEAGVTNLNITAAVADRGFFYAPDPSSQLACTIGGNIANNSGGAHCLKYGVTTNNLLGVRMVMIDGTIIDLGGNSLD | |||
| Full Sequence |
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| Protein Sequence Length: 483 Download |
| MSEVFMSAII FSEPDKAILD RRDAIVEHLA RLVSSDGLIT DRDECRAYET DAFAAYRKMP 60 LAVVLPTSTN EVSAVLRFCH DNGVKVVPRG AGTSLAGGAI PTEDAIVLGL SRMSRVLEIN 120 YDDRFIRVEA GVTNLNITAA VADRGFFYAP DPSSQLACTI GGNIANNSGG AHCLKYGVTT 180 NNLLGVRMVM IDGTIIDLGG NSLDSGGLDL LGVVVGSEGQ LGIVTEATVR ILRSAEAARP 240 VLFGFSSCDG AGNTVAEIIA AGIIPVAIEY MDKAAIEICE AFSKAGYPLD AEALLIIEVE 300 GSKAEMDATL DRIISIARAN GVQTVRESKS AIETAAIWKG RKSAFGATGR VADYLCMDGT 360 VPTGKLSYVL AQITEIVKRY GLRVANVFHA GDGNMHPLIL YNANDPAEQS KAEAAGNDIL 420 KLCVEVGGCL TGEHGVGIEK RDLMRHQFSE IDLAQQIRLR AAFDSKWLLN TDKVFPVDCR 480 NQT |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam01565 | FAD_binding_4 | 9.0e-35 | 60 | 196 | 137 | + FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan. | ||
| pfam02913 | FAD-oxidase_C | 1.0e-52 | 236 | 474 | 245 | + FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold. | ||
| COG0277 | GlcD | 6.0e-98 | 29 | 476 | 459 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| TIGR00387 | glcD | 2.0e-128 | 63 | 473 | 413 | + glycolate oxidase, subunit GlcD. This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity [Energy metabolism, Other]. | ||
| PRK11230 | PRK11230 | 1.0e-149 | 22 | 476 | 458 | + glycolate oxidase subunit GlcD; Provisional | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | YP_001977056.1 | 0 | 8 | 480 | 4 | 476 | glycolate oxidase protein, subunit D [Rhizobium etli CIAT 652] |
| RefSeq | YP_002543507.1 | 0 | 8 | 481 | 4 | 477 | glycolate oxidase, subunit GlcD [Agrobacterium radiobacter K84] |
| RefSeq | YP_002824941.1 | 0 | 11 | 480 | 7 | 476 | glycolate oxidase, subunit GlcD [Rhizobium sp. NGR234] |
| RefSeq | ZP_02165474.1 | 0 | 9 | 481 | 5 | 477 | putative glycolate oxidase subunit [Hoeflea phototrophica DFL-43] |
| RefSeq | ZP_06356974.1 | 0 | 6 | 482 | 1 | 477 | FAD linked oxidase domain protein [Rhodopseudomonas palustris DX-1] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3pm9_F | 0 | 25 | 474 | 17 | 475 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_E | 0 | 25 | 474 | 17 | 475 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_D | 0 | 25 | 474 | 17 | 475 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_C | 0 | 25 | 474 | 17 | 475 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_B | 0 | 25 | 474 | 17 | 475 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| HO388271 | 114 | 337 | 449 | 8e-36 |
| BP853374 | 124 | 291 | 413 | 1e-29 |
| CF306399 | 157 | 4 | 159 | 4e-29 |
| GE145663 | 238 | 11 | 247 | 8e-26 |
| GE179110 | 144 | 144 | 287 | 1e-23 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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