CAZyme Information: MGYG000002225_00850

Basic Information

• Species: CAG-873 sp900554265
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp900554265
• CAZyme ID: MGYG000002225_00850
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
671		74233.41	4.9982

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002225	2013827	MAG	United States	North America

• Gene Location: Start: 1021; End: 3036 Strand: +

Full Sequence      

MFKNLRPALGLALALAAAAPAMTAQTTNNDSRYLAWPAYEGEDLELAVDDSGTHFTLWSP
EAEKAEVLVYDTDRNGSPLMTLAMTRGEHGTWRASVPEKLYGKFYTFRVTVGGRTLDETP
GIWAKAAGTNGRRAAIVDFARTNPEGWDSDRGPALENITDAVIYEVHHRDFSMDPSSGIV
HKGKFLAMTEEGSTTPEGAKTGIDHLKELGVTHVHILPSYDYNSVDEANLQQNKYNWGYD
PYNYNTPEGSYSTDPANPEARIREMKEMIKALHDAGIGVVMDVVYNHTANNDDSNFSLTA
PGYFYRHRPDGSYSDASGCGNETASERPMMRDFIVNSVKYWADEYHIDGFRFDLMAIHDI
ETMNRVAEELKEVNPDIFVYGEGWTAGDSPLPADRRALKENVARMPGIAVFSDDIRDAVK
GHYSQAAGRGFATGAPGNEETVKIGIVASTAHPQVDYSKGNNSKFAYAAAPTQIINYVSC
HDDMNLTDKLAASMPGSTEAQRQRAARLAQTIVFTSQGTPFMFAGEEVFRSKKGVHNTYN
SPDSVNAIDWTLKTANADQFDYYRELIRLRKEHPAFRMTTADEVARNIEFDDVDTPNVVS
YSIKNNANGDQWKEIKLIFNGSDTPYTARIPRGDWKVIARDGQINADGLDTTRGGRLEVA
PVSALILARTN

Enzyme Prediction     

EC	3.2.1.41

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	203	527	4.4e-121	0.9965397923875432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	39	644	8	601	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	0.0	159	570	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	7.28e-147	38	671	62	693	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	6.63e-120	38	670	120	890	alpha-1,6-glucosidases, pullulanase-type. Members of this protein family include secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants. Both enzymes hydrolyze alpha-1,6 glycosidic linkages. 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 is closely homologous to, but architecturally different from, the Gram-positive pullulanases of Gram-positive bacteria (TIGR02102). [Energy metabolism, Biosynthesis and degradation of polysaccharides]
PLN02877	PLN02877	9.17e-110	52	631	216	923	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCP71427.1	0.0	28	668	14	654
QCD40325.1	0.0	28	668	14	654
QCD43695.1	0.0	13	670	2	656
QCD37019.1	0.0	33	669	2	639
ANU63796.1	0.0	21	669	22	671

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	9.89e-190	30	668	27	672	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	1.59e-188	30	668	27	672	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	1.59e-188	30	668	27	672	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
2WAN_A	3.60e-177	39	667	313	919	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
3WDH_A	6.13e-144	38	638	105	681	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	2.41e-163	39	669	221	842	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	9.40e-135	39	631	102	673	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2ZL64	1.10e-82	38	654	431	1105	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	1.34e-82	38	654	453	1127	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
A0A0H2UNG0	3.27e-82	38	654	446	1120	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000611	0.998438	0.000239	0.000293	0.000212	0.000186

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002225_00850.