CAZyme Information: MGYG000003570_02433

Basic Information

• Species: Treponema_D sp900769985
• Lineage: Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900769985
• CAZyme ID: MGYG000003570_02433
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
909		99770.26	4.5943

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003570	3193382	MAG	Fiji	Oceania

• Gene Location: Start: 31; End: 2760 Strand: -

Full Sequence      

MKKIFKIFSILALTSLLFSCADGLDESENRISTGSRAAFDSSLPKVEDGYLRINYFGTKA
ADLWIWDDFDESEIEKCSSWTSPGVSKTGTNGDFVYFDVKLSSSPAQVSFIVRSEASDAG
KLTENITFLFPTKYSEIFVNASGVYIDDECTKQASGLANAIITDEFKIKTTISGITLTED
NTKVLKADGTKIQISSISSSIITVSESLKEAGTVYVQYTDSNGTDMRIANFDSALIDKWF
SEVDISKFGYKDGVFTTWAPLASTAKVLLFAEAKDALSDTYTVAAEIPMTRNADGTWQTE
NVSATVGSNKYYQYSFMNNAVRYDVCDLWAKVASKDSKASAIEEMPSNSYEPLYKNPFGS
DGTETKLYNDAVIYEMHITDWSQAYRSEVQKDKPGTFKEITEALRTGGFAEHLKDLGITH
VQILPMFEYAVATKGTLNGSSVEFPTNDNAYNWGYNPYNYNTPESRYVQDMKDGTDAVSQ
MREMIAEFHKNGIAVIMDVVYNHTSGTGAGSIYDMTVPKYFYRMDSQGNYSNGSGCGNET
ATNNEMVKKFVIDSLKHWMEDYHINGFRFDLMGIHEKTTMAEIYEELSAIDKNVMVYGEP
WTGGTSAVKAGCTGAVDSGSYGVGAFDDDFRDAIKGAEFGGFNVGQVQSANADSGIVNGL
IGKSGKNKRNPTEYTGLALHYAECHDNFTLYDKLVYSLNFEKTQSNDSTGNVAKSWPASV
SEGQIDLIKKQNKLAAAYIFLSQGTPFINGGQEFMRTKKGDPDSYAADIKGGVFWGEIDE
VNAIDLSFKEKYADVFATYKGLIALRKDYSAFRNANTAEAETLSAGVTLYNVTADDGNFT
VVFNATDKTASFNAIEGKVVNVNGKLKMNGSYFGLGFNDVSSGVEKYSIAETASMVSTVP
AKSFVILKK

Enzyme Prediction     

EC	3.2.1.41	3.2.1.-	3.2.1.68	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	411	753	1.1e-92	0.9930795847750865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	4.23e-165	369	806	1	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	7.06e-154	254	853	22	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	1.13e-108	231	831	44	610	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02102	pullulan_Gpos	9.16e-74	31	853	97	954	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 (.
cd11326	AmyAc_Glg_debranch	2.97e-69	369	809	14	433	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSI02745.1	9.29e-251	1	909	1	878
QQA01551.1	2.87e-195	63	909	82	897
AEB13374.1	4.37e-179	255	909	37	613
QIB27254.1	9.09e-103	254	807	361	864
AEX86380.1	1.18e-100	62	858	54	829

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAN_A	2.46e-87	240	857	313	886	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
7LSA_A	1.63e-78	255	906	75	710	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	2.11e-77	255	906	75	710	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	2.18e-77	255	906	75	710	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	2.22e-77	255	906	75	710	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	7.70e-95	183	819	166	758	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	4.71e-71	223	821	88	628	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2UNG0	3.55e-60	49	853	244	1090	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64	8.12e-60	49	853	229	1075	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	8.57e-60	49	853	251	1097	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000000	1.000052	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003570_02433.