CAZyme Information: MGYG000000484_01746

Basic Information

• Species: Butyrivibrio_A sp000431815
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Butyrivibrio_A; Butyrivibrio_A sp000431815
• CAZyme ID: MGYG000000484_01746
• CAZy Family: GH13
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
871	MGYG000000484_11|CGC1	97357.65	4.3571

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000484	2428908	MAG	Fiji	Oceania

• Gene Location: Start: 61000; End: 63615 Strand: -

Full Sequence      

MKTSYRIVSLILTVIMVISLCACSNGKHDIQLETTGVGEPETIEDDSKRTSDDITIRLHY
FRDDGNYDGWNVWFWSTSDGKQYDFDKTVDDDGVTCTAHFDAGTRKVGFHVRLNDWDVKD
YADDRYIDTSKYITGTIDVYVVSGHSIVDVKYNSDCVKGTAVKSAVMSGDYESVTVFLSD
SAEDSTTVAIYDEDGNELESESVTIDERNKEKVIVKLKEKADWAGSYTVLLNGVCKFMIE
IPDFYSTEDFESKYSYTGNDLGASLEGNTTTFKVWAPMADGVTVNLYRSGDKSEDDLIKT
LSMNEGDSGVWSYVESQNLSGVYYTYTVERNGEKTEACDPYAKAVGVNGDRAMVIDMDST
DPDGWDKDVNPNKGMNYTDAIIYETHVRDFSIDESSGISAKGKYLGMTETGTKNQTGDAT
GLDHVKELGITHLQLSPVFDYATVDESNLSKAQYNWGYDPKNYNVPEGSYSSDPYNGDVR
IKEFKQMVKGLHDNGLSVVMDVVYNHTYNSKFCYNMIVPGYFHRPDSNGSACGNDVASER
IMVRKYIVESVVYWAREYHIDGFRFDLVGLIDAETIQEIRKALDEIDPSIILYGEGWSLD
TKTTKDYTFLATQNNVSRIDNFAMFNDSIRDALRGAVFVPTDKGYINGETSQTTSLKRYI
QGMVSWSRLPYQQVNYASCHDNLTLWDEINTSNASDSYESRVKQNLMSAAIIYTAQGIPF
IFSGEEMLRSKVSDDGTFDDNSYNSPDSVNSIKWDSLSGASQRKVYNYYKGLIEFRKAHP
AFCNMEKASSYYKFNKDVEDGVIAYELAPCNGESSDGIYVIHNPLSKDVTVELPDGTWTI
YVSGSTAGTKSLGNVSGEITVDSLTTTILVK

Enzyme Prediction     

EC	3.2.1.41	3.2.1.-	3.2.1.68	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	422	726	5.6e-109	0.9965397923875432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11341	AmyAc_Pullulanase_LD-like	0.0	378	776	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.
TIGR02104	pulA_typeI	0.0	250	851	2	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.
COG1523	PulA	3.42e-133	253	869	60	689	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103	pullul_strch	3.07e-121	254	871	121	896	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	2.49e-113	254	752	209	795	alpha-amylase/limit dextrinase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADL35847.1	3.52e-253	49	871	34	868
BBF44596.1	1.10e-238	240	871	10	648
BCN30228.1	1.66e-214	249	871	20	652
CDM69741.1	2.87e-212	37	870	128	989
CBL10489.1	1.37e-211	250	871	14	654

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JEQ_A	3.73e-167	250	844	30	629	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]
6JHI_A	5.84e-166	250	844	30	629	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
6JHH_A	5.84e-166	250	844	30	629	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
2WAN_A	5.68e-159	56	869	7	919	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
7LSA_A	1.80e-156	246	858	49	699	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	5.28e-166	53	871	20	842	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	8.33e-126	239	835	85	674	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
A0A0H2ZL64	4.24e-79	55	820	230	1049	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	5.10e-79	55	820	252	1071	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
A0A0H2UNG0	1.66e-78	55	820	245	1064	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000002	1.000056	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
7	26