CAZyme Information: MGYG000002671_00143

Basic Information

• Species: Treponema_D sp002478955
• Lineage: Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp002478955
• CAZyme ID: MGYG000002671_00143
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
921		100470.36	4.8524

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002671	2505445	MAG	United Republic of Tanzania	Africa

• Gene Location: Start: 181199; End: 183964 Strand: +

Full Sequence      

MKKITGIIAAVFAGAMLFSCANGLDGGTEANAKAAREAGTYKTDETLPSVANGYLRINTL
LTDAKDLWIWNDFDPSATALCKNWSEMAFPIKEKNGDFVYADIKLQDAPQQVSFILRKEF
NDNGKLTGDITFLFPSKYNEIFLKDGSGTIYIDSACTKEPTGLASAMITGEHAISATVKG
ISLSKENTKVFKADGTTEIKIDSISGSTITVYESLKENGTVYVQYSDENGADKRVANFDS
KLIDEWFNVDDSEIANFGYKDGVFTTWAPLSSSAKVLLFESAETVSGTNYKVAAEIPMTR
QANGTWKTKNVSSDVGANRYYKYSFMTNGVQYDVCDIWAKSASKDSVASAIEGVPANPES
SYTNPFGKNGSDTKLYNDAIIYEMHITDWSQAFRSSVEKDKPGTFKEITDALGTDGNGKF
GKHLRDLGVTHVQILPMFEYAVTTKGSSATDSDGKETVSFTENDNAYNWGYNPYNWNTPE
SRYVKDMTDGSDAISQMQEMIKAFHDAGIAVIMDVVYNHTAGTGKGSIYDMTVPKYFYRM
DSQGNYSNGSGCGNETASEHAMVRKYMIDSLKHWMNDYHINGFRFDLMGLHDKETMKEIY
DELYKIDKNVLVYGEPWTGGTAAVVNGATQAVSVTSDGGAGAFDDDFRDAIKGGEYGGFQ
IGQVQSANSDSGIIKGLLGEAGKNNRNTTGIPGLALHYAECHDNYTLFDKLVYSTIAPLS
GDFADKFADAYKVVIADKDKLNAIKAQNKLAAAYVLLSQGTPFINGGQEFMRTKQGDPDS
YAADKKGGVFWSNIDEVNAIDLTMKDEYSDVYNVYKGLIALRKNHPAFTKGNATAKTLAK
GVTVYNVKSDSEEFEVYFNASDKAYIISGANLSGNLGLGMNDVQIELGAKGKLVDISTGA
IVKTEAVLTTVPAKSFKILMK

Enzyme Prediction     

EC	3.2.1.1	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	423	769	7.6e-95	0.9896193771626297

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	7.67e-170	377	822	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	1.98e-166	263	867	22	584	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	3.75e-104	247	832	51	595	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02102	pullulan_Gpos	9.84e-83	53	903	112	1003	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 (.
PLN02877	PLN02877	6.03e-68	243	781	205	786	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSI02745.1	1.02e-258	46	921	38	878
QQA01551.1	5.69e-192	149	921	173	897
AEB13374.1	7.04e-181	225	921	6	613
AIY79639.1	1.77e-107	224	857	128	726
QJS18678.1	4.88e-106	88	868	184	939

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAN_A	3.37e-89	247	856	311	856	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
6JEQ_A	7.60e-85	238	828	26	564	Crystalstructure of Pullulanase from Paenibacillus barengoltzii complex with beta-cyclodextrin [Paenibacillus barengoltzii],6JFJ_A Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltohexaose and alpha-cyclodextrin [Paenibacillus barengoltzii],6JFX_A Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltopentaose [Paenibacillus barengoltzii],6JHF_A Crystal structure of apo Pullulanase from Paenibacillus barengoltzii [Paenibacillus barengoltzii],6JHG_A Crystal structure of apo Pullulanase from Paenibacillus barengoltzii in space group P212121 [Paenibacillus barengoltzii]
6JHI_A	1.03e-83	238	828	26	564	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
6JHH_A	1.03e-83	238	828	26	564	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
7LSA_A	1.29e-82	217	822	32	611	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	2.70e-98	189	833	166	756	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	8.19e-72	230	828	88	619	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2UNG0	1.72e-59	41	828	233	1034	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
Q9F930	4.15e-59	41	828	240	1041	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
A0A0H2ZL64	7.02e-59	41	828	218	1019	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 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	1.000046	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002671_00143.