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CAZyme Information: MGYG000003677_00637

You are here: Home > Sequence: MGYG000003677_00637

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species HGM11368 sp900772745
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; UBA3700; HGM11368; HGM11368 sp900772745
CAZyme ID MGYG000003677_00637
CAZy Family GH77
CAZyme Description Glycogen debranching enzyme
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1103 126155.94 5.4823
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003677 1306285 MAG United Republic of Tanzania Africa
Gene Location Start: 2583;  End: 5894  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.41 3.2.1.1 3.2.1.- 3.2.1.68

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH77 10 474 7.4e-144 0.951417004048583
GH13 655 967 6.3e-96 0.9930795847750865

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14508 PRK14508 0.0 1 492 2 497
4-alpha-glucanotransferase; Provisional
cd11341 AmyAc_Pullulanase_LD-like 4.67e-179 614 1010 4 406
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.
TIGR02104 pulA_typeI 6.82e-179 505 1017 12 533
pullulanase, type I. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases.
pfam02446 Glyco_hydro_77 1.70e-178 10 470 1 456
4-alpha-glucanotransferase. These enzymes EC:2.4.1.25 transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1,4)-alpha-D-glucan.
PLN02635 PLN02635 1.52e-129 4 496 28 530
disproportionating enzyme

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AIY78793.1 1.92e-129 505 1087 16 637
CDH91884.1 2.68e-129 505 1087 16 637
ACD23019.1 2.68e-129 505 1087 16 637
AJF34251.1 2.79e-127 505 1087 15 636
AJF31192.1 2.79e-127 505 1087 15 636

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7LSA_A 1.52e-112 505 1096 64 710
ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A 2.11e-111 505 1096 64 710
ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A 2.22e-111 505 1096 64 710
ChainA, Pullulanase [Ruminococcus bromii]
7LST_A 2.27e-111 505 1096 64 710
ChainA, Pullulanase [Ruminococcus bromii]
2WAN_A 1.68e-105 490 1099 304 921
Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P0A3Q0 3.97e-111 1 494 1 498
4-alpha-glucanotransferase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malQ PE=3 SV=1
P0A3Q1 3.97e-111 1 494 1 498
4-alpha-glucanotransferase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=malQ PE=3 SV=1
Q59266 5.22e-104 10 491 1 485
4-alpha-glucanotransferase OS=Clostridium butyricum OX=1492 GN=malQ PE=1 SV=1
C0SPA0 2.22e-102 505 1030 106 632
Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
O33840 8.13e-102 505 1017 225 752
Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.999858 0.000171 0.000001 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003677_00637.