CAZyme Information: MGYG000001527_01855

Basic Information

• Species: Fournierella massiliensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Fournierella; Fournierella massiliensis
• CAZyme ID: MGYG000001527_01855
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
638	MGYG000001527_17|CGC1	72510.69	5.9999

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001527	3828237	Isolate	not provided	not provided

• Gene Location: Start: 24626; End: 26542 Strand: -

Full Sequence      

MDFNSKAFARRFHYEGNDLGARLTEAGTEFRLWAPTAETVQLRLFRSGHEREAFETLALD
RGEKGMWFACIDRQLHGVYYDYLVTMEGNTRRTADPYARACGLNGRRSMVVDLAATDPEG
WQEDKAPARQLEDIVYEVHVREFSWAQSGGFPEHWRGKYKAFCCADTTLFDRGIQPTGLA
YLRQLGVTHVQLMPVYDYGSVDEAHPDDSFNWGYDPVNYNVPEGSYSTDPTRGEVRIREL
KELVQSLHRQGFRVIMDVVYNHTYHQDSWLERTVPGYYYRTWTDGSWSNGSGCGNDVASE
RSMCAKYILDSVLYWAEEYHMDGFRFDLMGLLDTDLMERIRAALDERFGRGEKLVFGEPW
AAGPTARKRGVRLADKKALAGLDPEIGAFCDGVRDAVKGPVMYREKPGFVNGGSGFEKRI
LHSITAWCGQARNFRAAAPSQVITYLSSHDDMTLWDKLVVTMDPQQNFDAPAPQVMRASQ
LAAAIYMTCQGRLFLLSGEEFGRTKQGEDNTHKAPIELNRLDWERAWQNRELVEYYQGLI
ALRKQLPALCDKTEQAGKRLLHSQVPAARCVTALLGNGGRWSKLLLAYNASSRPVELELE
EGEWELLADERSSFWWQEHPAVTGAQVQPMAAMILGKR

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	179	500	7.1e-103	0.9965397923875432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	0.0	134	543	4	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.
TIGR02104	pulA_typeI	0.0	7	595	1	582	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.
COG1523	PulA	2.77e-132	30	595	71	651	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	4.33e-107	15	523	124	728	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	1.53e-105	12	523	209	797	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHB23535.1	2.43e-263	3	638	12	644
QEI31027.1	2.43e-263	3	638	12	644
QUI96247.1	2.53e-259	3	638	11	643
AYA99650.1	4.92e-259	3	638	11	642
QJU43799.1	4.62e-205	3	638	10	655

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	2.64e-146	11	609	56	684	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	4.11e-145	11	609	56	684	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	4.34e-145	11	609	56	684	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	4.46e-145	11	609	56	684	ChainA, Pullulanase [Ruminococcus bromii]
6JEQ_A	9.59e-143	3	606	26	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	5.34e-129	12	635	219	840	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	5.81e-118	7	609	95	683	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2UNG0	3.23e-68	12	562	445	1047	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64	4.13e-68	12	562	430	1032	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q8GTR4	1.27e-67	12	529	202	796	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000050	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001527_01855.