CAZyme Information: MGYG000004099_00970

Basic Information

• Species: Eubacterium_R sp000433975
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp000433975
• CAZyme ID: MGYG000004099_00970
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1152	MGYG000004099_2|CGC4	125942.16	4.8205

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004099	1856381	MAG	United Kingdom	Europe

• Gene Location: Start: 447901; End: 451359 Strand: -

Full Sequence      

MKKKILSILLAICMAMCLLPTGVFADGKAFTAFGSDGNNGDGTVIDTAYDTAAQKLDNDY
GYTEYDLGANIIGNGKDEKMRFRFWSPTASQVKVNIFQRGTDDEQGATKIAAYTLKKLYE
NGKWTGVWEITLTGNWYSLYYTYSVTDADTGNTKDIADPYSRQFGRDGKRSYTINFDHYS
FKPEGWDGDSHVYFDSAKSRCVYRLDVASFTEDSSANVKNSGKFLGLTEAGTRYDDISDN
PSTGLDYIKQLGVTAVELDGVCDAENAFALNLQCATDQQSAVSELRQMIKVLHSAGLAVI
IKLPAGFVELNNGTFDNAVPNYYFRLNEAGEKLDGSGFGNELASERLMYRNWLITTLLGW
VNEYHIDGFSFEQSALIDSDTLSAAINAVSSVDNRIAFFADGECKTKNSHPSTVCTGETF
RRSTNANSAYLPSALIFEERSGKSLYAEICESLGVSSDQRNETAVKKAKFAAGLLAVSNR
IFYIDAGDEICAPELGRNVFEWKNIATYFDVFSYYRGLLQLRNTFPYFSSSEAQFKRGNI
LSASSSGNILVTGREANDWQTVSISYNATDKQTKEVALCDLRDWDIVASADFAGIDSRDK
LPESANNYFVLEPYSLKVAVDSSSFASAGFSSGTETLTLEFINEKTKEKLMPDMLLTGKS
GEGFILPNSGKPRLGNGYELHKTSSPVNGKFGETTKVTFEYGYIFDGIEDGGEYCSPAEF
KLKGINGVTKVKANGATLTPNGETYTLAGSGEQTVTVETGNGTHTIKVKLRSDHTYQFIT
ENGMYYKKCSACGQTTSPQAIPSIEITAPERVCAGQDCIVTVGTLPSGVTIENGLYEFEF
IGADFEITEKNGVWSGTVSHDWYQPDENKFDVCLVLKNTDGYIFTVRKTVNVLAEHTGGT
ATCTEKAKCEVCGESYGALDASNHTGTAEWFRNAQGHEKKYTCCGAVIVANEAHEWQNGV
CGECGYVCLHDDTDKNHVCDCCEKILSNHADADKDHVCDYCEKVISDHEDADKNHICDYC
EKVITNHTGGKATCAEKAICELCGKAYGELNASNHTNLVNFPAKAATTDAEGNIEYWRCE
GCGKYFADSAGTKEITAKDTVTGKLPSDKKSPQTGDGNSFTLGIALLFISGSVFTAFTVK
RKKSYQHGGNAK

Enzyme Prediction     

No EC number prediction in MGYG000004099_00970.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	245	412	3.2e-29	0.6539792387543253

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	6.45e-78	57	597	3	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	4.83e-47	202	522	5	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	3.75e-38	65	403	18	382	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	6.03e-34	39	402	98	526	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	9.42e-29	29	391	183	578	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACR73263.1	3.85e-137	18	1096	13	1190
QCT07748.1	4.66e-105	46	710	28	787
QCT05892.1	1.58e-71	3	739	2	820
APO32485.1	8.41e-67	47	646	21	693
QCT05893.1	9.98e-58	49	673	32	728

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	1.31e-108	3	701	5	792	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	3.48e-108	3	701	5	792	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	3.65e-108	3	701	5	792	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	3.74e-108	3	701	5	792	ChainA, Pullulanase [Ruminococcus bromii]
2WAN_A	1.29e-44	65	594	311	898	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	1.44e-43	62	618	220	839	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	2.10e-29	27	533	70	624	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	7.83e-18	67	392	208	572	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
B9G434	3.18e-14	65	377	106	450	Isoamylase 3, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA3 PE=2 SV=1
Q9M0S5	6.60e-11	156	388	185	444	Isoamylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA3 PE=1 SV=2

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
0.000310	0.998832	0.000256	0.000214	0.000192	0.000174

TMHMM  Annotations     

start	end
5	24
1120	1139