CAZyme Information: MGYG000000969_01066

Basic Information

• Species: Eubacterium_I sp900546495
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eubacterium_I; Eubacterium_I sp900546495
• CAZyme ID: MGYG000000969_01066
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1283	MGYG000000969_14|CGC1	140625.47	5.2025

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000969	2650866	MAG	Spain	Europe

• Gene Location: Start: 13121; End: 16972 Strand: -

Full Sequence      

MKYLKKIMAVALAAGMVFSGSVVDGRASSYRVNNYFDEAANTTIDELFFYDEDAYGKKLG
VTYEKTSTEFVVWAPVATDVKVNIYTTGSNEDENAFKVGTYVLEKLLRNGTWTGAWEITL
VGRWDDYYYDYTITNAKDIRYVDVNGNVSGSTFNKYQTADPYGVAASEDGQRSYVIDPST
VSPDGWSNDRHVYVDTAKANTVYKVSVKNFSTDPASGTTGGGKYSAFTETGATVNSAGEL
VSGIDYLKELGVTTVQLAPFADFASTDEYGEYDIQNFNVPESSYASKKSDSKTVIKECKE
MIQALHKAGISVVMEMPYTHTVSPKNSVLEKTVPGYFYRMVWRDSANGYTYYTTTDYDNE
CATERAMYRNYIVDSMAYWAKEYHVDGFSIDLISNVNTRRERNSTRENDWLSEIKTGLAK
KDSNLVIWGDDYQKADRQNKTSLYDSIINNIGGSDYGERNEKSVKIYKQTAAMKYATPGT
LYMDAGEEMCNSVNGTSLKDSNLVEWQDSAEFADVVSYYRGLMDIRKAFSPLARSQDIAS
KEAYVLTNTTKAAGEWNSMAVLNNETDAAKQITIPNADADSEWVIIANGESAGVVSLGEI
SGATVNVPAYTTMILVDKASFTGSAVSTTRGKVVVQYLLKDSKQPLREAITLQGTPGTGY
EVPANIKIPSGYTLLSKEGSEKGKYTAGTQTVTYYYSTIDANTVVDGIKNNGTYCENAKF
KVTSAAYTEVTVDGKKLTAGEDGYYTVSAADGVQKIALSDKDGYSIYLTITVNKNHTTDS
SDCTKESTCSVCHKTFPAQASHKFGDTWLKDDTYHWKVCENEGCKATSTKTKHSGTDDGD
CTTAVTCKDCGQIITEAKAEHTYGEWQSNGDGTHTRKCTAQGCTKEETKNCTGGEATCTK
KAVCTECQKEYGDLNPTNHSGSVEWVQTETTHQEKYNCCGAEVSAAENHTWENGHCSTCG
YGCNHTGGTATCIEKAICTICKLPYGEVDANHHTGTENWTQTATTHEKKYDCCGKVTVAK
ENHKWKDGVCETCGYVCVHSGGEATCTSGAICENCGKEYTAKDPSKHSGKVVWVQTESDH
RQVYDCCDAQVSASEAHDWEDGVCKVCDYQCKHTGGSATCVKKAECVICGEQYGVYNMSV
HEGLKFVEAKAATKTAEGNVEYWYCEDCGKYYIEQNGFVEVTKEQTVVAKLTDKKQDSNS
DDKKNHTPATGDTDNNKPTGSNGNDTKTTPTTDTKAANKAETTKKKSPKTADDNRMLVWF
ILFAVGGTAAGVTVYGHKRRTGR

Enzyme Prediction     

No EC number prediction in MGYG000000969_01066.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	244	438	4.5e-48	0.6401384083044983

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	5.10e-95	49	594	2	603	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	3.32e-77	202	526	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	4.45e-50	34	394	47	362	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PLN02877	PLN02877	7.34e-40	44	393	205	561	alpha-amylase/limit dextrinase
TIGR02102	pullulan_Gpos	3.00e-31	44	393	309	644	pullulanase, extracellular, Gram-positive. 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. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACR73263.1	0.0	1	1278	1	1387
QCT07748.1	4.23e-153	27	710	22	787
QCT05892.1	1.49e-102	4	772	1	860
APO32485.1	1.40e-92	27	637	15	688
QCT07019.1	1.78e-92	56	629	68	718

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	1.33e-158	1	697	1	793	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	1.95e-157	1	697	1	793	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	2.07e-157	1	697	1	793	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	2.13e-157	1	697	1	793	ChainA, Pullulanase [Ruminococcus bromii]
2WAN_A	1.87e-56	23	615	288	919	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	8.06e-45	51	432	217	566	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	3.63e-39	49	435	96	440	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	1.54e-19	44	462	198	621	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
Q9F930	1.62e-18	16	395	417	789	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
A0A0H2ZL64	2.10e-18	16	395	395	767	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
0.000438	0.998516	0.000435	0.000219	0.000201	0.000177

TMHMM  Annotations     

start	end
1256	1275