| Basic Information | |
|---|---|
| Species | Volvox carteri |
| Cazyme ID | Vocar20007651m |
| Family | GH13 |
| Protein Properties | Length: 1179 Molecular Weight: 128712 Isoelectric Point: 8.614 |
| Chromosome | Chromosome/Scaffold: 14 Start: 194434 End: 207410 |
| Description | isoamylase 1 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 353 | 570 | 4.3e-33 |
| APGTYAGMIEKLDHLQALGINAIELLPVFEFNELEYYSQIPGSKEYRYGVRQGDIQQLQLGSKERYNFWGYSTVNYFSPMGRYSAALAEGRPVRSTCDEF KQLVKECHKRGIEVLLDVVFNHTAEGNERGPTLSFRGLDNRVYYMLAPGGEYYNYRVFLHRATIPTTTNHNQLLPYRNPPTPRSGCGNTLNCNQPVVRQF ILDCLRYWVTEYHVDGFR | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1179 Download |
| MLLSGPGLTV GPARRQRQGL CNGNSGCTKT SVGHVLTAAA GSWTRDRRGI LPPLRVVSFE 60 LESPKLSSSP TAISTKKLST EPSGQPGSAL HGPVLTGRPE PLGASIDADT SKLHITTQLT 120 RSTDTRSVVA RDGPLATLRG GTPPGGLGFS HCNTTTTTTY YYYYYYHQLL ILILGAINFA 180 VFSSSATAVR LVLFTEADLT AGRATLEVPL DPTTNRTGDV WHVMLPNLRD DLLYGYRVDG 240 LHQDTDKEGP GHRHDQSHVV LDPYAVAVLS RRRWGQLGPN LPYGEPGVLG LMPTWPQAAA 300 ALPSGRYSSS SFSHQPHFDW EGDRPLNLPM ESLVIYEAHV RGFTAHESSG VGAPGTYAGM 360 IEKLDHLQAL GINAIELLPV FEFNELEYYS QIPGSKEYRY GVRQGDIQQL QLGSKERYNF 420 WGYSTVNYFS PMGRYSAALA EGRPVRSTCD EFKQLVKECH KRGIEVLLDV VFNHTAEGNE 480 RGPTLSFRGL DNRVYYMLAP GGEYYNYRVF LHRATIPTTT NHNQLLPYRN PPTPRSGCGN 540 TLNCNQPVVR QFILDCLRYW VTEYHVDGFR RRWFCSEENG PFFSAGGGGA AAAASFAILI 600 MLLLLLLLLL LPKRLPRFDL ASILTRAPSA WHPQQYDEET GQPVAMSSGG ALVSAEGIMT 660 DGAGVPTGTP LPDPPLVEAI SEDPVLRNTK LVAEAWDCDG LNQVGAFPHY GGRWSEWNGK 720 FRDVVRNFIK GTDGPWAGDF ASAVCGSPNI YASSQPQESD WWGNNGGRQW RGGRGPSASI 780 NFVTAHDGFT LADVVSYNNK HNEANGEDNR DGEAHNNSWN CGEEGPTSKW EVNRLRQRQM 840 RNMSAALLLS CGVPMITMGD EYGHSKGGNN NTYCHDSELN YVSTCSYRSR PPPGPSSLFQ 900 GFPVLPSCPA FTQLPHQPDW SETSRLVAFT LSDGKGGGLY VAFNTSHMPR LLKLPNWAGR 960 LWQPLLDTSK HGGVRSVDKT SPSQPPPNPQ AELRTAFAAC RFAGVAPYDF LAADGVLSVA 1020 DVAAARRSMS MWTADHTYPV LPWSCIVLVS APEDPTSTNM IRRAATQPAS GRSGGGSSDT 1080 AGPRNPMSWA SNFINSQHLL VAPASPAGAR TTARHTARAR RHIATRGVRQ RVAARGGVVR 1140 KRLRNDRCHR HGGLIDDVGL VAIVAADVVR CSLRRRRR* 1200 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd11341 | AmyAc_Pullulanase_LD-like | 5.0e-49 | 334 | 570 | 249 | + Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of limit dextrins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. | ||
| PRK03705 | PRK03705 | 9.0e-128 | 177 | 879 | 712 | + glycogen debranching enzyme; Provisional | ||
| TIGR02100 | glgX_debranch | 8.0e-173 | 175 | 969 | 838 | + glycogen debranching enzyme GlgX. This family consists of the GlgX protein from the E. coli glycogen operon and probable equivalogs from other prokaryotic species. GlgX is not required for glycogen biosynthesis, but instead acts as a debranching enzyme for glycogen catabolism. This model distinguishes GlgX from pullanases and other related proteins that also operate on alpha-1,6-glycosidic linkages. In the wide band between the trusted and noise cutoffs are functionally similar enzymes, mostly from plants, that act similarly but usually are termed isoamylase [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
| cd11326 | AmyAc_Glg_debranch | 0 | 318 | 882 | 570 | + Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. | ||
| COG1523 | PulA | 0 | 177 | 978 | 827 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005975 | carbohydrate metabolic process |
| GO:0043169 | cation binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAP85534.1 | 7e-21 | 1 | 129 | 1 | 126 | isoamylase [Chlamydomonas reinhardtii] |
| GenBank | AAP85534.1 | 0 | 175 | 1062 | 109 | 875 | isoamylase [Chlamydomonas reinhardtii] |
| RefSeq | XP_001697539.1 | 7e-21 | 1 | 129 | 1 | 126 | isoamylase, starch debranching enzyme [Chlamydomonas reinhardtii] |
| RefSeq | XP_001697539.1 | 0 | 175 | 465 | 109 | 373 | isoamylase, starch debranching enzyme [Chlamydomonas reinhardtii] |
| RefSeq | XP_001697539.1 | 0 | 537 | 1062 | 375 | 833 | isoamylase, starch debranching enzyme [Chlamydomonas reinhardtii] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2vuy_B | 0 | 177 | 570 | 31 | 361 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| PDB | 2vuy_B | 0 | 679 | 932 | 384 | 640 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| PDB | 2vuy_A | 0 | 177 | 570 | 31 | 361 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| PDB | 2vuy_A | 0 | 679 | 932 | 384 | 640 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| PDB | 2vr5_B | 0 | 177 | 570 | 31 | 361 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
