CAZyme Information: MGYG000001925_00230

Basic Information

• Species: Phocaeicola sp900544675
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900544675
• CAZyme ID: MGYG000001925_00230
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
664	MGYG000001925_2|CGC1	73604.15	5.4042

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001925	3441241	MAG	Denmark	Europe

• Gene Location: Start: 73218; End: 75212 Strand: -

Full Sequence      

MKLKHLLILPVLAAMSCQSVKHDYESFADYPVVEGDWEEMVYAPEGTKFALWAPTAEEVN
LKLYAEGQGGEPVQTIPMKAAEDGLWRTEVAEDLNGQFYTFDVKVKGNWLGDTPGVWAKA
VGVNGDRAAVLDLDATDPEGWDKDVRPELKSFADIVLYEMHHRDFSIDSLSGITHRGKFL
ALTEEGTRNADGQKTGIDHLKELGVTHVHILPSFDYSSVDETRLDTPQYNWGYDPKNYNA
PEGSYSTDPYKPDVRIREFKQMVMALHRAGIRVVMDVVYNHTAVTDGSNFERTVPGYFYR
QTPEGGFANASACGNETASERAMMRKFMVESVKYWVEEYHVDGFRFDLMGIHDLETMRAI
RKALDEIDPTIYIYGEGWAAGAPQLPMDSLAMKNNIDRLTRIAAFSDEFRDSLRGPFGND
AQGAFLAGLKGHEAGIRFGIAGGVQHPQVNGEGGHQVPKFWALQPTQFISYVSCHDDMCL
ADRLKATMPQASAGVRKSLQKLALTAVLTSQGVPFIFAGDEVMRDKQGVHNSFNSPDEIN
AIPWSLKKTNRDLFDYVSGLIAMRRCHPAFRLGDADKVRACLEFLPATDDNVVAFRLKGK
PEGETWSDITVVLNASSRAAQVEMPAGTWQVVCRDGRINPSQGLGTVSGGAVSISPRSAM
ILHR

Enzyme Prediction     

No EC number prediction in MGYG000001925_00230.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	197	521	1.6e-115	0.9965397923875432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	29	638	3	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	154	564	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	1.38e-142	49	664	71	691	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	1.85e-134	44	617	134	844	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	4.18e-119	42	626	219	924	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADY34912.1	0.0	1	664	1	664
AII63226.1	0.0	1	664	1	664
ALK85304.1	0.0	1	664	1	664
QQY43875.1	0.0	1	664	1	664
QEW36945.1	0.0	1	664	1	664

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	3.76e-193	27	631	30	625	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	6.04e-192	27	631	30	625	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A	6.04e-192	27	631	30	625	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
2WAN_A	5.76e-149	41	664	321	921	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
7LSA_A	1.38e-140	40	661	66	710	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	6.42e-158	41	664	228	842	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	1.07e-134	41	625	109	673	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	2.21e-82	42	550	212	796	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2ZL64	8.64e-69	51	624	451	1076	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	9.39e-69	51	624	473	1098	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
0.000002	0.001287	0.998748	0.000000	0.000001	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001925_00230.