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Basic Information | |
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Species | Volvox carteri |
Cazyme ID | Vocar20007569m |
Family | AA5 |
Protein Properties | Length: 1380 Molecular Weight: 150166 Isoelectric Point: 8.416 |
Chromosome | Chromosome/Scaffold: 14 Start: 1927185 End: 1942374 |
Description | glyoxal oxidase-related protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA5 | 41 | 551 | 0 |
SSLATSDESSADPTAALSPSRQRQFRDLVSPGGRRLLEAAAYALDNARSVTAAPEDRRQIAPSRLLQRSSALDLNLRMVDRDETASVLGDITNAGMLART YLQLPPSPPRPPRPPPPSPKPPPPSPRPMPPSPVPPSPFPSPQPPSPAPSPPKPPASPPYNSSSDDYATDASDVFVPFRNDGPVSLPLLMDNYPEANGQW VLKAVGNVVAVHMSLIPGTDKFFFMERPSGRHPDRSSNIVGYYDYLTNRFTNINYTDSVFCAGHTVTQDGHVMIVGGHISKSGYGDGLKAVRILSRRTAT LYRITNMSYPRWYPTATLLPSGKVTIMGGTVLPGAGSAKNPIYEIWDPANPTQLDVRRQSAGLVSQTKDIYYPNTYVLPTGDLLIMCAAYGEITEPLSGT LRTVLPSWSNVAGDLQLEYPYAGTSVMLPLTPYNNYTPEVVVFGGQYDKARINTTASRLALRLKVSYNATTNLYSFGGGWTAEKMPLPRVMGDAVVLPNG KVVVLNGAVLG | |||
AA5 | 834 | 1366 | 0 |
NQPDAYGQWILKAVGNVVAVHLCMVPGTDKFFFMERPSGRHPDGGNNIAGYYDYLTNRFTNVNYTDSVFCAGHTVTQDGHVMVVGGHIAKSGYADGLKGV RIFSRRTLTFKRITSMSYPRWYPTATLLPSGKVTIMGGTVLPGAGTGKNPIYEIWDPANPTVLITRNQSNGLVTKTNDIYYPNTYVLPTGDLFIFCNRYG EITEPMTGTVRTTLPSWSTVAKGIFTEYPFTGTSVMLPLTPDNGYTPEVVYFGGQFSYGWINTTASRLALRIKVVYDPATRNYTFGDGWTAEKMPLPRVM GDAVVLPNGKVVVLNGAVKGLAGDSASGGVAKANEPNLWPVLYDPDAPSGSRMRLMSRSMIPRLYHSTVSLTTDGSLLVAGCDRCDKYWWTTPGGISKSP TSFAEYRIEVFRPPCWFNVTAKPQIISMDDATWDEYDGVNVMQYGEPFALQYSMFYATDSVTSAVLVSPSSTTHSTNMNQRVVGLEILAQDVDARRLVLN GPPDINIAPPGWYMLFLLNGDVYGQSAWVRLPG |
Full Sequence |
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Protein Sequence Length: 1380 Download |
MMLPAYSPRF VPLVLLLLLL LTSITCNASL ASPRRQVHLA SSLATSDESS ADPTAALSPS 60 RQRQFRDLVS PGGRRLLEAA AYALDNARSV TAAPEDRRQI APSRLLQRSS ALDLNLRMVD 120 RDETASVLGD ITNAGMLART YLQLPPSPPR PPRPPPPSPK PPPPSPRPMP PSPVPPSPFP 180 SPQPPSPAPS PPKPPASPPY NSSSDDYATD ASDVFVPFRN DGPVSLPLLM DNYPEANGQW 240 VLKAVGNVVA VHMSLIPGTD KFFFMERPSG RHPDRSSNIV GYYDYLTNRF TNINYTDSVF 300 CAGHTVTQDG HVMIVGGHIS KSGYGDGLKA VRILSRRTAT LYRITNMSYP RWYPTATLLP 360 SGKVTIMGGT VLPGAGSAKN PIYEIWDPAN PTQLDVRRQS AGLVSQTKDI YYPNTYVLPT 420 GDLLIMCAAY GEITEPLSGT LRTVLPSWSN VAGDLQLEYP YAGTSVMLPL TPYNNYTPEV 480 VVFGGQYDKA RINTTASRLA LRLKVSYNAT TNLYSFGGGW TAEKMPLPRV MGDAVVLPNG 540 KVVVLNGAVL GVPLLFIMLC YTTYHMGEVR YWWTTPGGIS KSPTSFAEYR IEVFRPPCWF 600 NVTAKPQIIS MDAATWDEYD SVNVMQYGEP FALQYSMFYA NDTVTSAVLV SPGSTTHSTN 660 MNQRVVGLEI LAQDVDARRL VLNGPPDINI APPGWYMLFL LNGDVYGQSA WVRLPVSDFC 720 STCLIGASHL SATCRTIHIM ARSNRVTPGA SHKPPSRPPP RKPSPPPPKP PPPSSPPPNS 780 PPSPRPPSPQ PSPPKPPASP PYNATSDDEG PGPSDGNSST PGDGNVNLPI VPDNQPDAYG 840 QWILKAVGNV VAVHLCMVPG TDKFFFMERP SGRHPDGGNN IAGYYDYLTN RFTNVNYTDS 900 VFCAGHTVTQ DGHVMVVGGH IAKSGYADGL KGVRIFSRRT LTFKRITSMS YPRWYPTATL 960 LPSGKVTIMG GTVLPGAGTG KNPIYEIWDP ANPTVLITRN QSNGLVTKTN DIYYPNTYVL 1020 PTGDLFIFCN RYGEITEPMT GTVRTTLPSW STVAKGIFTE YPFTGTSVML PLTPDNGYTP 1080 EVVYFGGQFS YGWINTTASR LALRIKVVYD PATRNYTFGD GWTAEKMPLP RVMGDAVVLP 1140 NGKVVVLNGA VKGLAGDSAS GGVAKANEPN LWPVLYDPDA PSGSRMRLMS RSMIPRLYHS 1200 TVSLTTDGSL LVAGCDRCDK YWWTTPGGIS KSPTSFAEYR IEVFRPPCWF NVTAKPQIIS 1260 MDDATWDEYD GVNVMQYGEP FALQYSMFYA TDSVTSAVLV SPSSTTHSTN MNQRVVGLEI 1320 LAQDVDARRL VLNGPPDINI APPGWYMLFL LNGDVYGQSA WVRLPGTAPR LDDFFATLK* 1380 1440 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07250 | Glyoxal_oxid_N | 5.0e-16 | 885 | 1087 | 216 | + 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. | ||
pfam09118 | DUF1929 | 7.0e-18 | 625 | 714 | 91 | + 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. | ||
pfam09118 | DUF1929 | 6.0e-18 | 1275 | 1364 | 91 | + 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-24 | 1273 | 1364 | 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. | ||
cd02851 | E_set_GO_C | 2.0e-24 | 623 | 714 | 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. |
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_001701421.1 | 0 | 221 | 549 | 156 | 484 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
RefSeq | XP_001701421.1 | 0 | 570 | 715 | 553 | 697 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
RefSeq | XP_001701421.1 | 0 | 804 | 1375 | 137 | 707 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
RefSeq | XP_001701422.1 | 0 | 219 | 549 | 165 | 495 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
RefSeq | XP_001701422.1 | 0 | 801 | 1378 | 145 | 721 | glyoxal or galactose oxidase [Chlamydomonas reinhardtii] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2wq8_A | 0.0001 | 888 | 1352 | 236 | 646 | A Chain A, Glycan Labelling Using Engineered Variants Of Galactose Oxidase Obtained By Directed Evolution |
PDB | 2eid_A | 0.0001 | 888 | 1352 | 214 | 624 | A Chain A, Galactose Oxidase W290g Mutant |
PDB | 2eid_A | 0.002 | 299 | 702 | 226 | 624 | A Chain A, Galactose Oxidase W290g Mutant |
PDB | 2eic_A | 0.0002 | 888 | 1352 | 214 | 624 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |