| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM5G877941_T03 |
| Family | AA4 |
| Protein Properties | Length: 249 Molecular Weight: 26410.3 Isoelectric Point: 7.001 |
| Chromosome | Chromosome/Scaffold: 2 Start: 234092343 End: 234102994 |
| Description | FAD-linked oxidases family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA4 | 96 | 226 | 2e-21 |
| QEFIDELASFLGDNITLDYEERSFHGTPQNSFHKAVNLPDVVVFPSSQDEVQRIVMACNKHKVPIVPYGGATSIEGHTLAPHGGVCIDMTLMKKIKSLNV EDMDVVVEPGVGWIELNEYLKPYGLFFPLDP | |||
| Full Sequence |
|---|
| Protein Sequence Length: 249 Download |
| MATSLLRLSR HRRALLAISS VRLALSTQPH VPSPSPSPTP SSARRLPHFL SFLAAAAAAA 60 AGGATVALCD SGLDHRVGGK DSADLVVRGE RKFVPQEFID ELASFLGDNI TLDYEERSFH 120 GTPQNSFHKA VNLPDVVVFP SSQDEVQRIV MACNKHKVPI VPYGGATSIE GHTLAPHGGV 180 CIDMTLMKKI KSLNVEDMDV VVEPGVGWIE LNEYLKPYGL FFPLDPGPGA TIGGMCATRC 240 SGSLAVSL* 300 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK11230 | PRK11230 | 3.0e-10 | 133 | 242 | 112 | + glycolate oxidase subunit GlcD; Provisional | ||
| TIGR00387 | glcD | 2.0e-21 | 137 | 242 | 108 | + 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]. | ||
| pfam01565 | FAD_binding_4 | 1.0e-31 | 134 | 246 | 115 | + 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. | ||
| COG0277 | GlcD | 2.0e-36 | 101 | 246 | 149 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| PLN02805 | PLN02805 | 6.0e-122 | 43 | 246 | 206 | + D-lactate dehydrogenase [cytochrome] | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
| GO:0016491 | oxidoreductase activity |
| GO:0050660 | flavin adenine dinucleotide binding |
| GO:0055114 | oxidation-reduction process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| DDBJ | BAG90549.1 | 0 | 68 | 248 | 71 | 251 | unnamed protein product [Oryza sativa Japonica Group] |
| GenBank | EEC81560.1 | 0 | 45 | 232 | 52 | 245 | hypothetical protein OsI_24999 [Oryza sativa Indica Group] |
| RefSeq | NP_001142976.1 | 0 | 1 | 246 | 1 | 246 | hypothetical protein LOC100275430 [Zea mays] |
| RefSeq | XP_002461502.1 | 0 | 1 | 246 | 1 | 265 | hypothetical protein SORBIDRAFT_02g003640 [Sorghum bicolor] |
| RefSeq | XP_002524111.1 | 0 | 38 | 246 | 31 | 246 | d-lactate dehydrogenase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2uuv_D | 0.00000000005 | 97 | 242 | 93 | 251 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 2uuv_C | 0.00000000005 | 97 | 242 | 93 | 251 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 2uuv_B | 0.00000000005 | 97 | 242 | 93 | 251 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 2uuv_A | 0.00000000005 | 97 | 242 | 93 | 251 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 2uuu_D | 0.00000000005 | 97 | 242 | 93 | 251 | A Chain A, Alkyldihydroxyacetonephosphate Synthase In P212121 |
| Hydropathy |
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