CAZyme Information: MGYG000001957_01138

Basic Information

• Species: UMGS268 sp900540705
• Lineage: Bacteria; Firmicutes; Bacilli; Acholeplasmatales; Anaeroplasmataceae; UMGS268; UMGS268 sp900540705
• CAZyme ID: MGYG000001957_01138
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
897	MGYG000001957_21|CGC1	99807.73	4.8014

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001957	1806938	MAG	Denmark	Europe

• Gene Location: Start: 22829; End: 25522 Strand: +

Full Sequence      

MKKILLFLLFLLTGLSLVSCGGGTTDDGGDKPDDGDKPQPVDPELPESTEDLGFAIHYDQ
TTMDGEKYHWNLWLWETGKDGADYQFNGKDSYGIVARYKWEEFSTTAKQSGIGFIVKENK
VWAEGPAKDGDSDRFIDFSSLERDKYGYYNVYLKYEDETVYTSATGEVNDMVSYFSLAYN
VVKGFQIWFQTNKAFESYEITLGDQVVFSDTVGLDKLESKDDTRVVYNLGKELPDLFNTY
SLKVTFKESGKSIEKVADNSIIYSTQAFAEAYTYTGELGAIYRAESTTFRVWSPISTSIQ
LRIYDIGTPKSLGGNDIFTEFAMTKGEKGVWEYTFNGDCAGKYYTYVVTNATYKNAEVVD
PYAKSTGLNGLRGMIVDFSKTNPEGWENVSVHPYSSTELTVYETHIADLTSSTTWGGTAA
NAKLYTGFYEAGTTYTEGDVTVSTGFDHIKELGVNAVQILPFFDQANEERVGKRAFNWGY
NPLNYNALDGIYSADPTDGYLKIKEFKNLVKAYNEAGINIIMDVVYNHVAGLEKCNFDVL
MPKYYFRYTSAGASNGSGCGNETASEMPMFRKFMVDSTEFWASEYKLGGFRFDLMGIHDV
KTMNELSKNLHENVSEHITVYGEPWAGGTIALGSGHTAAAQVSMNKYEGYGCFNDKMRDA
LIKGGLSGKAERGWITNSSKVSSGDVTNIKAGLRGLVLSTNKTLEPEKCVNYVTCHDNYT
LYDRIKAAGIKDEATIKKMAMLSNSVVFTSQGVTFMLAGEEFLRTKGGNENSYNASYKVN
ELNYSLKVKNLDMFNAYKKLIQLKHNKGLFGKSGEECKEITIQTNKDGSLIYYDLVDTVN
QVSYRIVHSNGVAAQDKQVDLAGYTLYLDTLGKSDLTLTAQTTLDAYQTIIASKPLA

Enzyme Prediction     

EC	3.2.1.1	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	447	761	9.8e-94	0.9930795847750865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	267	810	1	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	6.05e-169	397	804	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.
COG1523	PulA	1.62e-98	272	810	61	591	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02102	pullulan_Gpos	6.01e-81	44	766	108	814	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	4.28e-75	270	790	207	803	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOS39053.1	5.71e-249	1	894	1	887
VEU82346.1	6.91e-167	2	872	3	858
QWB95757.1	1.31e-151	48	849	24	844
VEU81131.1	1.32e-150	56	801	34	788
BCR36445.1	7.17e-147	41	893	22	875

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	1.20e-119	249	873	34	695	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	1.75e-118	249	873	34	695	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	1.84e-118	249	873	34	695	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	1.89e-118	249	873	34	695	ChainA, Pullulanase [Ruminococcus bromii]
6JEQ_A	6.64e-108	268	804	30	558	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	3.98e-118	55	819	24	761	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	6.62e-81	262	804	90	613	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2ZL64	1.32e-56	56	773	233	942	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	1.37e-56	56	773	248	957	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
Q9F930	7.77e-56	56	766	255	957	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	0.000244	0.999816	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001957_01138.