y
Basic Information | |
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Species | Chlamydomonas reinhardtii |
Cazyme ID | Cre05.g243450.t1.3 |
Family | AA5 |
Protein Properties | Length: 968 Molecular Weight: 101446 Isoelectric Point: 7.9005 |
Chromosome | Chromosome/Scaffold: 5 Start: 1562792 End: 1570687 |
Description | glyoxal oxidase-related 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 |
AA5 | 60 | 779 | 0 |
AAISAAAATSARLTAAEVAGGAASAAAATDGGSEQLAWSADPQLQQGQTFGHRRSLLKAKKGDSNAGSSGSSISGMTIIAGAAATPPLAPKKHKKSPPPR SPPPRSPPPPRRHKSPPPVRPLTEPPLPAPPTVLETTDAPPPRSPPPQPAPPPPPPPSPTPSPPPPSPSPPSPPPPSPRPPSPRPPPPPSPRPPVPPPRP PPPSPPPPSPPPPSPPPTSLPPPPLPSPEESSGPSDGYDGEYGGEDGYMGGGSGAGNATDADNSMDEPEWPPFPPPHPRDANAPSPPPPPPPAPGSRHGQ YEFIGSANIIAVHLMAVPGTDNFLFMERPSGRHPDGSHNIAGFLNLPTRAWTHLYSPDGLFCAGHTFLDTGDLLIVGGHQANAGYPDGMKSIRTFNRTCT DLQLRKVVEMAWKRWYPSATLLPDGNVLVMGGTQGVGAGTANNPFWEMFYPSNGTTRTFAMKPNYLDSAEQVYYPFNYVLPSGLLFTFCGRSGFILDYTN NTWMQNLPRLRGWATTQYPFTGTSVMLGLYPETGYTAEVVLFGGQAERATRNLSTIAAKQAQRLTLSAYDPVTRNYSFGPTGSWVGENLGSPRLMGDSVL LPNGKVVLLNGAQTGLAGDSASGGDTRANYPVLFAELYDPDRPQGQRVRSLGFSRIPRMYHSTACLTTNGTILVAGCDRCQRFVVDEGWTYDPSPTGKAD YRLEIFHPPFVFFPSDRPII |
Full Sequence |
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Protein Sequence Length: 968 Download |
MLLPLLLLLL SAPFIASAAS AASAAEEASA EAVADHSRGL KALGGGHWHV QRRPQLAAAA 60 AISAAAATSA RLTAAEVAGG AASAAAATDG GSEQLAWSAD PQLQQGQTFG HRRSLLKAKK 120 GDSNAGSSGS SISGMTIIAG AAATPPLAPK KHKKSPPPRS PPPRSPPPPR RHKSPPPVRP 180 LTEPPLPAPP TVLETTDAPP PRSPPPQPAP PPPPPPSPTP SPPPPSPSPP SPPPPSPRPP 240 SPRPPPPPSP RPPVPPPRPP PPSPPPPSPP PPSPPPTSLP PPPLPSPEES SGPSDGYDGE 300 YGGEDGYMGG GSGAGNATDA DNSMDEPEWP PFPPPHPRDA NAPSPPPPPP PAPGSRHGQY 360 EFIGSANIIA VHLMAVPGTD NFLFMERPSG RHPDGSHNIA GFLNLPTRAW THLYSPDGLF 420 CAGHTFLDTG DLLIVGGHQA NAGYPDGMKS IRTFNRTCTD LQLRKVVEMA WKRWYPSATL 480 LPDGNVLVMG GTQGVGAGTA NNPFWEMFYP SNGTTRTFAM KPNYLDSAEQ VYYPFNYVLP 540 SGLLFTFCGR SGFILDYTNN TWMQNLPRLR GWATTQYPFT GTSVMLGLYP ETGYTAEVVL 600 FGGQAERATR NLSTIAAKQA QRLTLSAYDP VTRNYSFGPT GSWVGENLGS PRLMGDSVLL 660 PNGKVVLLNG AQTGLAGDSA SGGDTRANYP VLFAELYDPD RPQGQRVRSL GFSRIPRMYH 720 STACLTTNGT ILVAGCDRCQ RFVVDEGWTY DPSPTGKADY RLEIFHPPFV FFPSDRPIIL 780 APSLDASPPP PPRASPPPPP PPPPTGTKAK QPLPSQHDDL GVAVVMGYGT THQIRYAWPA 840 GFAGPQPGSS IGMNATAPPA ADPYDVWTPG VITRVVLSAP CSNTHSFDMN QRLVGLEILS 900 NTPDPSTGSS SGTTGSSSGS SSTVAGGVLT VRSPPDINIA PPGMYHMFLV NGDVYSSAVW 960 VRLARPQ* 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam09118 | DUF1929 | 8.0e-14 | 872 | 963 | 93 | + 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. | ||
cd02851 | E_set_GO_C | 3.0e-18 | 872 | 963 | 93 | + 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. | ||
pfam07250 | Glyoxal_oxid_N | 1.0e-19 | 420 | 603 | 194 | + 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. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_001691237.1 | 0 | 448 | 966 | 1 | 424 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
RefSeq | XP_001698053.1 | 0 | 363 | 963 | 225 | 731 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
RefSeq | XP_001701419.1 | 0 | 334 | 963 | 109 | 654 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
RefSeq | XP_001701526.1 | 0 | 346 | 792 | 371 | 788 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
RefSeq | XP_001701526.1 | 2e-17 | 857 | 967 | 786 | 876 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |