CAZyme Information: MGYG000001828_00211

Basic Information

• Species: UBA4951 sp900542595
• Lineage: Bacteria; Firmicutes; Bacilli; RFN20; CAG-826; UBA4951; UBA4951 sp900542595
• CAZyme ID: MGYG000001828_00211
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1038	MGYG000001828_2|CGC1	115860.2	4.1861

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001828	1066613	MAG	Denmark	Europe

• Gene Location: Start: 18103; End: 21219 Strand: +

Full Sequence      

MKFPKLVLPIVAFLSVCGLAGCGTPDGGGNPVGDSTPGPVNSNGDTSSTPAVPLPEGWQD
TIRIYYRNDTASYNNLCLWVWATGIEGSIYSFTNEGNPDEYGLYCDIDLKAAPFNRLELT
GISFIVRNKTNWDGQSQDVIINFNDYSGTLETVDGRERITVYSWGLTNNNVMVSSNRMDA
LGDRIGSMYFEDWRTLRVKGTGDPTNRDESEVGLISSYKLYAFPSAYYQMTAAQQIGHKK
DYLVKEGTPASNDFTISFDEDIALQTDYIIEAYMAQNPSQAKSMGASFTNLYPSQKFIDE
YTYNGHDLGVTTSEKGRPTIKVWAPTAANVAVRLYTYGTPENLALEGMVTDDLRARSSDM
TPIENGVWTYTLGGAESRTFDFYTLEVSTGGTTVETIDPYAKSSGINGVRGALLTDSEWD
ETDPEGFREAIANIDETCPIDSPNDLSVYEVHIRDFTADETWKGKEPRGTYNAFIEEGVT
YGDNGQSVKTGFDSLKELGITAVQLLPVFDQDNEERTLKLTIDGETFEQGPGYNWGYNPL
NYNVVEGSYSTDPYSPTTKIIEFKKLIQKCAENGIRVIMDVVYNHMSSVGNNSFNKLMPG
YYFLTDDNGSYVDLTGVHNTFDTSRPMAKNFVVDSVTFWAEEFGIKGFRFDLMGAITTDT
MRAVKDALYDVDPNIVVYGEPWRGNNPEGIDYDKYAGDYQVFRDLTDNGKGVVGCFNDCG
RNALKGDTSWGNPAPSYGFMTQNEDLSEETIYNAAVVYIGEERDITNNANPLPTRPDQVI
NYVSCHDNYTLYDQLNYCYNGGKGASTDSNPGVMDALIATQSYVLLSQGMSFIHGGEEIF
RQKLMYSDNYYWDTIADNDYVTLPDKDSEGNEIRLIRNSYAYGDEVNSYKWDRKLTYIDE
FERYAEACNLRKELVKQGALGVDYDVIQGSYQRDGQTFKYSRLWDDIISRKEDGTLRSIL
AAQTEWTQIPDGAYSNDIYVFLGGRMDNGVDSLEDIGIGNGQFEVLYDSLGIFGKTMNIT
NNKLGIHGYQMVMLKRVG

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	493	838	6.2e-87	0.9930795847750865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	2.24e-153	297	913	2	528	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	3.91e-147	444	911	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	6.81e-91	322	912	73	586	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PLN02877	PLN02877	4.96e-78	298	877	205	822	alpha-amylase/limit dextrinase
TIGR02102	pullulan_Gpos	1.65e-77	53	893	108	868	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
VEU81131.1	7.81e-119	60	912	30	792
SQH56883.1	5.03e-109	60	912	29	791
ABX81281.1	6.27e-109	60	912	40	802
QLY39684.1	2.55e-107	65	912	77	831
BCR36445.1	8.45e-106	48	912	20	790

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAN_A	5.26e-96	298	913	308	826	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
6JEQ_A	1.89e-87	296	912	29	559	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]
6JHH_A	2.51e-86	296	912	29	559	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	2.51e-86	296	912	29	559	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
3WDH_A	1.24e-82	294	913	97	616	Crystalstructure of Pullulanase from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDI_A Crystal structure of Pullulanase complexed with maltotriose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDJ_A Crystal structure of Pullulanase complexed with maltotetraose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	2.97e-76	59	913	20	747	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	6.50e-75	297	912	96	614	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2ZL64	4.14e-55	41	893	195	989	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	1.00e-54	41	893	210	1004	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
Q9F930	1.79e-54	41	893	217	1011	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	1.000056	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001828_00211.