CAZyme Information: MGYG000000479_00131

Basic Information

• Species: Treponema_D sp900541995
• Lineage: Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900541995
• CAZyme ID: MGYG000000479_00131
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
880		96231.32	4.7852

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000479	2347794	MAG	Fiji	Oceania

• Gene Location: Start: 143880; End: 146522 Strand: -

Full Sequence      

MKKTIALMLTALLSLGIGLSGCSDGINSNPGTSTDKNGMSVDPNLLSVQEGQIRINCAYS
NAQNLWVWDDFAASEVDKCADWNTSDAVTLTGTNGDFKYFDVKLADNPKQVSFIIRSAKG
NNKLTEDLIFIFPNKYNEIYVVDGKIMVTTSDKSTGKVSLSNPKGLASGSIVDENTIKLI
GDGISLSDKNITVKNGDKTLTVSSISGMTLTTSESLKNYGMVEVSYTDEMGTDTITAIPD
DTLLDNWFNMDITKLGYADGVFTTWAPLASKVQVLLYETAASLGDSTYLPKEISMSRQTD
GTWKTEDVAGDVSGNNYYKYRIRNGNYSYDVCDIWAKVASKNSEATQIVSINDSSAKPAG
WNSEYENPFSGSSVKYYSDAIIYEMHIRDWSMAMDNSSSGSFDEIADAMKVGGTLYNHLK
DLGVTHVQILPMFEYAKVGTDDTAYNWGYNPYNWNTPETRYVKSMTDGTDAVKSMRSMIQ
AFHDAGIAVNMDVVYNHTSGTKNGSIYDMTVPKYFYRTNGDTYLNGSGCGNETNSEHEMF
KKYMIDSLKHWMTDYHINGFRFDLMGVHDTSTMEEIYKELVKIDQNVMVYGEPWTAGDKN
ASIATEGAISVGNTNGVAAFDDDFRDAIKGAEYGGFNKGQVQGFYNDSGIIKGLSGASGK
NKRNTTGRPALSLHYVECHDNYTLADKLCYSTVGSSIIGKDDIVEYFKSFSELNETKQAL
VKAQNKLSAAYVFLAQGTPFINGGQEFMRTKKGNPDSYAADTKGGYKWSETEILNCNAID
LNFKDTYSDVYNTYKGLIALRKANSVAFGHNGGARAEKVSAGVTKYTTGDFLVYFNATDA
AVPIIDASGYSTAVDVSSGTPTDATVPTNVAAKSFVILKK

Enzyme Prediction     

EC	3.2.1.41	3.2.1.68	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	417	746	3.9e-91	0.9930795847750865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	4.14e-161	261	808	22	532	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.
cd11341	AmyAc_Pullulanase_LD-like	1.70e-156	379	801	2	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.
COG1523	PulA	1.17e-98	256	878	65	689	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02102	pullulan_Gpos	7.33e-72	50	841	111	950	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	3.02e-64	265	758	229	786	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSI02745.1	1.06e-263	48	880	46	878
QQA01551.1	1.02e-238	65	880	82	897
AEB13374.1	1.08e-201	243	880	14	613
CBL13024.1	4.09e-104	262	805	35	559
VCV21250.1	1.44e-103	262	805	32	556

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	1.01e-85	262	804	52	561	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	1.39e-84	262	804	52	561	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
6JHH_A	1.39e-84	262	804	52	561	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
2WAN_A	4.18e-83	244	801	318	824	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
7LSA_A	1.02e-73	262	848	75	675	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	2.71e-87	64	802	38	746	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	1.58e-63	261	804	116	616	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2UNG0	1.53e-53	51	758	244	957	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64	1.98e-53	51	758	229	942	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	2.06e-53	51	758	251	964	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	0.000004	1.000045	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000479_00131.