CAZyme Information: MGYG000000488_01375

Basic Information

• Species: Anaeroplasma sp900767915
• Lineage: Bacteria; Firmicutes; Bacilli; Acholeplasmatales; Anaeroplasmataceae; Anaeroplasma; Anaeroplasma sp900767915
• CAZyme ID: MGYG000000488_01375
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
723		83197.39	7.6501

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000488	1945837	MAG	Fiji	Oceania

• Gene Location: Start: 11332; End: 13503 Strand: -

Full Sequence      

MSEFIYCDFLENYTVGFKVDSNALEGSLYLNDKLISTSKLKKNCKNHKIKFSINDFDARG
IYKVKVLLENGDMVESIVNNISLYNTNYFDKKYTYNGNLGAIYSNEKTSFRLWAPICSRV
ILRVYESGTPLAIDKEKGNDSILYSIPMEYTQNGVWECDINGDLEGKYYTYIITNYKNEN
VEVVDPYAKSCGISGRRGMIVDFSKTNPEGWNEVKVIPYKRTEIVVYETHISDITSSSSW
TNDIELLKYQKKFKGAYTKGTSYTEGNISVKTGFDHIKELGVNVVQLLPFFDRANDETKM
SFNWGYDPLNYNTLEGSYSMNPYDGYERIKEFKELVKAYNEAGINIIMDVVYNHVFDALK
SNFEIITPGYFFRHNKDLSLSNGSGCGNETRSEMPMFRKFMIESTEFLAREYKLFGFRFD
LMAVHDYETMNLLVSNLKNKVNENIVVYGEPWVGGDSTLSPKLRASQANGKKFNYYGQFN
DKYRDALIMGGVKKDFELGWIDTNKKIKNSELKKIINGIKGYTVGDNSSIYDPNKTVNYV
TCHDNHTLFDRFKAVGIFDDSVIKKMAMLSNSMILTSNGTSFILAGEEFLRTKGGDSNSY
ISSYKVNELDYSLKIKNLDMFKNYQKLIEFKKNVSDLHLTNKELLDNINIVVSKDFNQIS
YRIKNSSNNREYLVIHNNGYKSDTLPLLDLRGYNLYLSINGSIELKEFTKPLPYQTIIVY
KNY

Enzyme Prediction     

No EC number prediction in MGYG000000488_01375.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	275	588	2.6e-94	0.9930795847750865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	88	695	1	594	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	9.28e-166	222	631	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	5.62e-97	92	713	60	658	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	2.93e-81	90	617	116	734	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	3.43e-73	90	612	206	798	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOS39053.1	1.15e-211	22	721	186	887
VEU82346.1	1.68e-158	69	677	221	835
VEU81131.1	3.79e-149	50	722	195	888
BCR36445.1	1.31e-147	52	682	196	842
QWB95757.1	3.80e-146	28	687	177	854

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	6.58e-111	90	701	54	685	ChainA, Pullulanase [Ruminococcus bromii]
2WAN_A	2.73e-110	92	687	310	883	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
6JEQ_A	6.92e-110	68	632	12	559	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]
7LSR_A	9.73e-110	90	701	54	685	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	1.02e-109	90	701	54	685	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	5.70e-100	93	715	219	842	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	6.20e-78	89	632	96	614	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2UNG0	1.40e-50	90	636	442	995	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64	1.85e-50	90	636	427	980	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	3.39e-50	90	636	449	1002	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1

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
1.000058	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000488_01375.