CAZyme Information: MGYG000002303_01406

Basic Information

• Species: Ruminococcus_E sp003438075
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp003438075
• CAZyme ID: MGYG000002303_01406
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1245	MGYG000002303_3|CGC2	134323.15	4.6869

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002303	2565731	Isolate	China	Asia

• Gene Location: Start: 66280; End: 70017 Strand: -

Full Sequence      

MFLKRTLAVLLSATMLFGMTSLSTTAATTDTEAVSAGNYYNASYLENYASNAYNEKNLGA
NYTKSSTEFKVWSPEASAVKVKLYATGSDSESGAAVLGTYNLKKNSSTGMWSVTVNGDLK
NTYYTYLVTVNGTTNETQDVYSKATGVNGNRSMVVDLDSTDPEGWDSDNHVLFNNAQEAV
VWEVHVRDFSVSDTSGVSDDNKGKYLAFTEGGTKISSDTSANAVSTCADYLVKSGINCVQ
LMPVYDFGSVDETITGSATNRNWGYDPVNYNVPEGSYSSNPYDGNVRITEFKQMIQALHD
RGISVVMDVVYNHTYVTEGSCFTDTVPNYYYRKTSSSVYSNGSGCGNETASDKLMYRKYM
IDSILYWASEYHIDGFRFDLMGLHDITTMNQIRSSLDNLYSDGSGKKILMYGEPWTGGSS
AISDGCFQSKASQLDARVGMFCDSYRDAIKGGTNDASTGFIQGNNGKTYTVVNGVKGQCF
GAKAPSQTIAYADAHDNLIMWDKMVLSNGSKDWNSTSSSLTDQMKATMGLLLTSQGIVFM
TAGSEFCRTKQGDHNSYKSADSINAIDWTRLKTYSETADYYKGLLKIRENYSPLKGGNFS
TPTFQSSYGYVVAYTYSNNTAGEWGKVCVLVNSGTQACTIGLDGSDWTVVANGTKAGLES
LGTVSGKSYSIPARSTCVLVQSSTFGNLQNAEPTYGTLKVNHVDENGDVLKSTSATYKTG
TTYRALPDTTLLYDYNLVNTTGTTTGKVESGKTYTVTFTYKSSGISSGYLTVNYVNANGT
KVKDSVKNKMRSGDEYSVSPATIQGYQLDTDSFPANTSGTFSGTDTTITFKYKKLNSTST
VVHYKKPSSWSDVRCYSYTDDGKNPTGEWNTATVMTSEGDGWYKCTVPASACYVMFHPTS
NTAQEPGQGASGYPASGEVWINNGAITFTGTVITSHIDIATGKKIAADVVSEKTKVTSSD
TYTTSAVAGKNVITPLNATGNYFAGVINVVYLYDSGEVPTTAAPTTQPTTAKPTTQPTTA
TVAPTQTVAPTVQPTTPAEKIWIGDVDMDGRISINDVSLLQMFISEQTTFTDKQLIAADA
NDDGSVDVIDATLVQMYLVYNIADGSLVGQYKYIVQPTQPTTQASTAAPTTQPTTAEPTT
EPTTTPSGTYTVTFTNSLNWDGTIYCYYWTSGSQGEVAWPGTKMNFVENNDYGQAVYTLT
VPSSCDSVIFTNGSSQTVDINTGSKDTDYYAKTTKTGTGYNVGTW

Enzyme Prediction     

No EC number prediction in MGYG000002303_01406.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	229	545	2.9e-105	0.9930795847750865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	53	660	7	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	177	588	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	8.02e-125	69	679	71	689	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	1.01e-97	58	682	128	897	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	3.39e-93	58	569	215	798	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT07019.1	6.32e-218	5	697	15	720
QCT05893.1	7.94e-204	3	834	3	830
APO32485.1	1.79e-199	44	685	26	672
QCT05892.1	4.47e-192	3	813	1	819
QCT07748.1	1.60e-177	52	760	43	777

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	6.16e-199	4	750	5	783	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	9.47e-198	4	750	5	783	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	1.01e-197	4	750	5	783	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	1.04e-197	4	750	5	783	ChainA, Pullulanase [Ruminococcus bromii]
2WAN_A	2.69e-136	53	681	313	921	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	1.59e-116	53	666	220	828	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	6.10e-100	53	589	101	614	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	2.34e-55	58	613	208	832	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2UNG0	3.10e-50	58	590	451	1030	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64	6.81e-50	58	590	436	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
0.000772	0.995934	0.002617	0.000244	0.000209	0.000189

TMHMM  Annotations     

start	end
7	29