CAZyme Information: MGYG000000392_01016

Basic Information

• Species: Ruminococcus_E sp003521625
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp003521625
• CAZyme ID: MGYG000000392_01016
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1228	MGYG000000392_3|CGC6	132896.4	4.5849

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000392	2042501	MAG	Sweden	Europe

• Gene Location: Start: 191534; End: 195220 Strand: -

Full Sequence      

MKFRKPLSLLLSAAMITSMASFAANAVVTNNAEVSAGSYYNATYLETYANSAYNETGLGS
VYSKTSTTWKTWSPDATAVKVKLYKTGSDSESGAGVIGTYPLTKNSTTGVWSTTLTGDYK
DVYYTYLVTVNGSTNETQDVYSKAVGVNGNRSMVVDLDSTDPDGWDSDNHVLFDSAAEAV
VWEVHVRDFSASSTSGVSAENQGKYLAFAEGGTTLNSDTSANAVSTGIDYLVEQGINCVQ
LMPVYDFQSVDESKASSSSNRNWGYDPQNYNVPEGSYSSDAYNGNTRITEFKQMIQALHD
RGISVVMDVVYNHTYTTEGSCFSKTVPDYYYRKKSSSTYSNGSGCGNETASDKLMYRKYM
IESLKYWAEEYHIDGFRFDLMGIHDITTMNTIRTELDNLYADGSGKKILMYGEPWTGGTV
AISDGCSQAKAASLDARVGMFCDSYRDAIKGDTNGTGKGYVQGTTSKTSTVVRGIQGKGF
KAKAPSQTIAYADAHDNLILWDKIIRSNSSSAWNSTDEKFKGQLKEAMALIMTSQGIPFM
TAGSEFCRTKQGDHNSYKSSDAINAIDWTRVKTYSDVAAYYKGLLEIRENYTPMKDTKFN
TPSFQSSSGYVVAYTYSNSKSDEWGKVCVLVNSGTQANSIDLDGSGWTVVADGTNAGLKS
LGTVSGSSYSIGAKSTAVLVESSTFSRLKTAETQYGTLTINHVNDKGEVLKTSTAKYREG
STYRALPDSTILFDYSLKSTEGTTSGKVVGGENYSVTFVYSSTGIASGYLTVKYVNSSGT
EIKDAASYHLRAGDSYEIPVAAIQGYQLDTDKYPAESYGTFGGSDKTITFTYKDLENTSS
TVHYYNANNWTDVRCYAYTDGGEEPNGKWASATKMTSEGNGWFVCTVPAISAYVMFHPTS
GSAQEPGSGEQGYPVAGEAWIQNKTVTFSSKVITSHIDVATGKKIAADVIDNQAKTTSES
SYTTSALSGRTDVITPSNAQGKYSAGIVNVVYLYTSSQPITTAPPATTQPSTTVPPSGKI
LIGDTDDNGAITVADASTIQKYLADLVVFSDRQIIAGDCDGGGLVGIKDATLIQMYCAEY
RNTGNVGKYVGGVEETTAPITTEPVTTQPTTAPPTTQPTTVPPTTVPTPETYTVKFSNAQ
HWSGTIYCYYWTDGEVAPVAWPGTEMTFVENNDYGEVVYSVEVPSDADFIIFNNNDSQTV
DIPFDGSVLNFYAMSEIDENWRHLYDTW

Enzyme Prediction     

No EC number prediction in MGYG000000392_01016.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	228	545	4.9e-107	0.9965397923875432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	58	660	12	605	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	178	588	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	8.85e-127	68	682	70	697	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	5.38e-99	17	569	92	729	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	6.29e-92	58	569	215	798	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT07019.1	1.10e-217	66	687	79	712
APO32485.1	2.57e-194	64	685	46	672
QCT05893.1	1.05e-190	64	832	55	828
QCT05892.1	9.22e-180	64	758	60	781
QCT07748.1	1.07e-171	64	880	55	953

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	3.10e-186	64	761	70	793	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	4.73e-185	64	761	70	793	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	5.03e-185	64	761	70	793	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	5.19e-185	64	761	70	793	ChainA, Pullulanase [Ruminococcus bromii]
2WAN_A	7.85e-129	64	666	324	907	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	2.93e-111	67	666	234	828	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-99	67	630	115	660	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	2.31e-58	72	613	222	832	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2UNG0	4.16e-54	72	590	467	1030	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64	9.13e-54	72	590	452	1015	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 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
0.000407	0.998793	0.000186	0.000217	0.000185	0.000169

TMHMM  Annotations     

start	end
7	29