| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | Cre03.g152050.t1.2 |
| Family | AA5 |
| Protein Properties | Length: 644 Molecular Weight: 67489.6 Isoelectric Point: 6.0849 |
| Chromosome | Chromosome/Scaffold: 3 Start: 1512048 End: 1518933 |
| Description | glyoxal oxidase-related protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA5 | 12 | 642 | 0 |
| HSLAVLTAVLLLAAVALLLPAAAGAAADLMPPPPSPPPPPQHQSPAAVAEVQGAAAVAARAQGANSTAMQLGELDFRKKKAKKPAAAAVSRSSWRTLPFM STAVPALLAVLPPYDQYLAIENSKTTTTSLLDLEQETATAMKSLVNSFCGAPVHQEDGGLILVGGHHGYKNGIADGRDKIQLFGLDPDPAFSLAHPLRWN RWYPAVTTLEDGRVLVVGGSYKADAGSLPPFSEIVDPKALDQESETLPTPQNFVDNAGMQWFAFMHTLPRGHVLWWGDRGGSISDVASQAVLADLPELPE EVTHRTAYPYTASVLVLPYRPEEDYRATLMIFGGAEGGAGTDTPAVSTSLRLELRECDSAASGYCAVPWEVEEMGVPRVMGDSVLLPNGKVLLLNGAQWG RAAYSSSGQKAGGQASHPANQPLIYEPWRPAGERYFHVAFNPIPRMYHSTACLHRTGEVIAAGCDTCGENVAGLTSAMTPNPKGLLEKRLQMFTPAEIAP GVARPVITLAPASIARDQTFTVEFTYDPPAAAEVAQGGGTGGSGSSPPAPAVTAASLVTPCATTHSVGWNQRVVFLKVLSPDSGSDSSGTRSLTLAAPPS SHPGLSPPGYHLLFLVTSDGGYSQGVWLTVT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 644 Download |
| MKPPQRPPVA AHSLAVLTAV LLLAAVALLL PAAAGAAADL MPPPPSPPPP PQHQSPAAVA 60 EVQGAAAVAA RAQGANSTAM QLGELDFRKK KAKKPAAAAV SRSSWRTLPF MSTAVPALLA 120 VLPPYDQYLA IENSKTTTTS LLDLEQETAT AMKSLVNSFC GAPVHQEDGG LILVGGHHGY 180 KNGIADGRDK IQLFGLDPDP AFSLAHPLRW NRWYPAVTTL EDGRVLVVGG SYKADAGSLP 240 PFSEIVDPKA LDQESETLPT PQNFVDNAGM QWFAFMHTLP RGHVLWWGDR GGSISDVASQ 300 AVLADLPELP EEVTHRTAYP YTASVLVLPY RPEEDYRATL MIFGGAEGGA GTDTPAVSTS 360 LRLELRECDS AASGYCAVPW EVEEMGVPRV MGDSVLLPNG KVLLLNGAQW GRAAYSSSGQ 420 KAGGQASHPA NQPLIYEPWR PAGERYFHVA FNPIPRMYHS TACLHRTGEV IAAGCDTCGE 480 NVAGLTSAMT PNPKGLLEKR LQMFTPAEIA PGVARPVITL APASIARDQT FTVEFTYDPP 540 AAAEVAQGGG TGGSGSSPPA PAVTAASLVT PCATTHSVGW NQRVVFLKVL SPDSGSDSSG 600 TRSLTLAAPP SSHPGLSPPG YHLLFLVTSD GGYSQGVWLT VTP* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd01965 | Nitrogenase_MoFe_beta_like | 0.008 | 149 | 222 | 80 | + Nitrogenase_MoFe_beta_like: Nitrogenase MoFe protein, beta subunit_like. The nitrogenase enzyme catalyzes the ATP-dependent reduction of dinitrogen (N2) to ammonia. This group contains the beta subunits of component 1 of the three known genetically distinct types of nitrogenase systems: a molybdenum-dependent nitrogenase (Mo-nitrogenase), a vanadium-dependent nitrogenase (V-nitrogenase), and an iron-only nitrogenase (Fe-nitrogenase). These nitrogenase systems consist of component 1 (MoFe protein, VFe protein or, FeFe protein respectively) and, component 2 (Fe protein). The most widespread and best characterized of these systems is the Mo-nitrogenase. MoFe is an alpha2beta2 tetramer, the alternative nitrogenases are alpha2beta2delta2 hexamers having alpha and beta subunits similar to the alpha and beta subunits of MoFe. For MoFe, each alphabeta pair contains one P-cluster (at the alphabeta interface) and, one molecule of iron molybdenum cofactor (FeMoco) contained within the alpha subunit. The Fe protein contains, a single [4Fe-4S] cluster from which electrons are transferred to the P-cluster of the MoFe and in turn, to FeMoCo, the site of substrate reduction. The V-nitrogenase requires an iron-vanadium cofactor (FeVco), the iron only-nitrogenase an iron only cofactor (FeFeco). These cofactors are analogous to the FeMoco. The V-nitrogenase has P clusters identical to those of MoFe. In addition to N2, nitrogenase also catalyzes the reduction of a variety of other substrates such as acetylene The V-nitrogenase differs from the Mo-nitrogenase in that it produces free hydrazine, as a minor product during N2-reduction and, ethane as a minor product during acetylene reduction | ||
| pfam09118 | DUF1929 | 0.0001 | 515 | 641 | 127 | + Domain of unknown function (DUF1929). Members of this family adopt a secondary structure consisting of a bundle of seven, mostly antiparallel, beta-strands surrounding a hydrophobic core. The 7 strands are arranged in 2 sheets, in a Greek-key topology. Their precise function, has not, as yet, been defined, though they are mostly found in sugar-utilising enzymes, such as galactose oxidase. | ||
| pfam07250 | Glyoxal_oxid_N | 8.0e-6 | 124 | 345 | 229 | + Glyoxal oxidase N-terminus. This family represents the N-terminus (approximately 300 residues) of a number of plant and fungal glyoxal oxidase enzymes. Glyoxal oxidase catalyzes the oxidation of aldehydes to carboxylic acids, coupled with reduction of dioxygen to hydrogen peroxide. It is an essential component of the extracellular lignin degradation pathways of the wood-rot fungus Phanerochaete chrysosporium. | ||
| cd02851 | E_set_GO_C | 5.0e-10 | 511 | 641 | 131 | + C-terminal Early set domain associated with the catalytic domain of galactose oxidase. E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_001695542.1 | 0 | 1 | 643 | 1 | 618 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
| RefSeq | XP_001695587.1 | 0 | 157 | 642 | 71 | 530 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
| RefSeq | XP_001695699.1 | 0 | 138 | 642 | 117 | 585 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
| RefSeq | XP_001695700.1 | 0 | 138 | 641 | 31 | 495 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
| RefSeq | XP_001701523.1 | 0 | 138 | 642 | 265 | 728 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2wq8_A | 0.0000000001 | 95 | 631 | 193 | 649 | A Chain A, Glycan Labelling Using Engineered Variants Of Galactose Oxidase Obtained By Directed Evolution |
| PDB | 1t2x_A | 0.0000000002 | 95 | 631 | 171 | 627 | A Chain A, Glactose Oxidase C383s Mutant Identified By Directed Evolution |
| PDB | 2eic_A | 0.0000000005 | 95 | 631 | 171 | 627 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| PDB | 2vz3_A | 0.0000000006 | 95 | 631 | 171 | 627 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| PDB | 2vz1_A | 0.0000000006 | 95 | 631 | 171 | 627 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
