CAZyme Information: MGYG000003534_00001

Basic Information

• Species: Treponema_D sp900769325
• Lineage: Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900769325
• CAZyme ID: MGYG000003534_00001
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
427		46432.81	5.0699

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003534	2560433	MAG	Fiji	Oceania

• Gene Location: Start: 643; End: 1926 Strand: -

Full Sequence      

MIAEFHKNGIAVIMDVVYNHTSGTGGGSIYDMTVPKYFYRMDSQGNYSNGSGCGNETATN
NEMVKKFVIDSLKHWMNDYHINGFRFDLMGIHEKTTMAEIYEALSEIDKNVMVYGEPWTG
EESAVKSGCTGAVKAGSYGVGAFDDDFRDAIKGAEFGGFNIGQVQSANSDSAIKNGLIGK
SGNNNRNSTGFTGLALHYAECHDNFTLYDKLVYSLDVTNTKKSDSTGNIAKAWPTPISDG
QIDLIKKQNKLAAAYIFLSQGTPFINGGQEFMRTKKGDPDSYAADLKGGVFWGEIDEVNA
IDLSFKETNKDVYSTYKGLIALRKSSTAFTNGTESTAKTLSKGVTLYNAKSDSEEYEVIF
NASENDYVLTDVSIEGNLGLGMKDYEVSFGRKGKLVTISEKDGSVNTADTVTTVSTVPAK
SFVILKK

Enzyme Prediction     

EC	3.2.1.1	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1	270	1.1e-70	0.7785467128027682

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	1.37e-127	1	323	112	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	1.35e-103	1	370	234	585	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.
COG1523	PulA	7.19e-77	1	425	270	689	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11326	AmyAc_Glg_debranch	8.86e-45	1	325	114	432	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.
TIGR02102	pullulan_Gpos	3.27e-41	1	333	560	902	pullulanase, extracellular, Gram-positive. 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. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQA01551.1	3.11e-135	1	427	510	897
QSI02745.1	1.52e-134	1	427	491	878
AEB13374.1	1.04e-129	1	427	229	613
QJS18678.1	1.72e-69	1	370	575	939
QPJ84848.1	9.87e-69	1	329	250	570

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAN_A	8.98e-60	1	358	537	856	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
7LSA_A	2.96e-54	1	330	308	618	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	3.77e-53	1	330	308	618	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	3.83e-53	1	330	308	618	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	3.86e-53	1	330	308	618	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	1.20e-63	1	329	449	751	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	7.09e-48	1	329	321	619	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2ZL64	1.60e-30	1	329	681	1019	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	2.17e-30	1	329	696	1034	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
Q9F930	2.17e-30	1	329	703	1041	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000066	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003534_00001.