| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G117369_T03 |
| Family | AA4 |
| Protein Properties | Length: 537 Molecular Weight: 58445.4 Isoelectric Point: 6.3948 |
| Chromosome | Chromosome/Scaffold: 7 Start: 13397796 End: 13405223 |
| Description | FAD-linked oxidases family protein |
| 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 |
| AA4 | 104 | 275 | 5.7e-22 |
| IAYFKSILGENGVVQDEDRVAVANVDWMGKYRGASQLVLLPKTTTEVSKILSYCNTKRLAVVPQGGNTGLVGGSVPVFDEVIVGLAGMNKIISFDNVNGI LTCEAGCVLENLSTFVENEGFIMPLDLGAKGSCHIGGNISTNAGGLRFIRYGSLHGNVLGLEVVLADGTILD | |||
| Full Sequence |
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| Protein Sequence Length: 537 Download |
| MPRREAARLL RRLGPIAVQS PKRGFSGMPH NQYESTNHAV NSYRRFHWIP SVQHPLCGPT 60 SSGGIYEGQR SANKACEVQK RTFGSAATQF QRNPAYSVLN SDDIAYFKSI LGENGVVQDE 120 DRVAVANVDW MGKYRGASQL VLLPKTTTEV SKILSYCNTK RLAVVPQGGN TGLVGGSVPV 180 FDEVIVGLAG MNKIISFDNV NGILTCEAGC VLENLSTFVE NEGFIMPLDL GAKGSCHIGG 240 NISTNAGGLR FIRYGSLHGN VLGLEVVLAD GTILDMLTTL RKDNTGYDLK HLFIGSEGSL 300 GVVTKISVLT PAKLSSTNVA FLSCNDYTSC QKLLLAARRS LGEILSAFEF MDHHCIDLAM 360 QHLEGVQNPL PASPYKFYVL VETTGSDESS DKTKLEAFLL RSMEDGLVAD GVIAQDISQA 420 SNFWRIREGI SEASVKVGAV YKYDLSITVE KLYDIVEEMR CRLGDNAEVL GYGHLGDGNL 480 HLNIVSSKYD DNILAQIEPF VYEWTSAQRG SISAEHGLGL MKAEKIHYSK SPEAVSV 540 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK11230 | PRK11230 | 1.0e-30 | 129 | 527 | 421 | + glycolate oxidase subunit GlcD; Provisional | ||
| pfam01565 | FAD_binding_4 | 7.0e-35 | 139 | 275 | 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 | 2.0e-43 | 313 | 535 | 231 | + FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold. | ||
| TIGR00387 | glcD | 4.0e-65 | 141 | 535 | 406 | + 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]. | ||
| COG0277 | GlcD | 2.0e-97 | 106 | 533 | 439 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| 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 | BAC79943.1 | 0 | 1 | 537 | 1 | 534 | putative actin interacting protein [Oryza sativa Japonica Group] |
| GenBank | EEC81643.1 | 0 | 1 | 537 | 1 | 534 | hypothetical protein OsI_25178 [Oryza sativa Indica Group] |
| GenBank | EEE66707.1 | 0 | 1 | 537 | 1 | 553 | hypothetical protein OsJ_23376 [Oryza sativa Japonica Group] |
| RefSeq | NP_001141496.1 | 0 | 1 | 537 | 1 | 537 | hypothetical protein LOC100273608 [Zea mays] |
| RefSeq | XP_002268002.1 | 0 | 74 | 537 | 61 | 524 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3pm9_F | 0 | 99 | 537 | 13 | 456 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_E | 0 | 99 | 537 | 13 | 456 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_D | 0 | 99 | 537 | 13 | 456 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_C | 0 | 99 | 537 | 13 | 456 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| PDB | 3pm9_B | 0 | 99 | 537 | 13 | 456 | A Chain A, Crystal Structure Of A Putative Dehydrogenase (Rpa1076) From Rhodopseudomonas Palustris Cga009 At 2.57 A Resolution |
| Hydropathy |
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