CAZyme Information: MGYG000002836_01056

Basic Information

• Species: Anaerocolumna aminovalerica
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerocolumna; Anaerocolumna aminovalerica
• CAZyme ID: MGYG000002836_01056
• CAZy Family: CBM41
• CAZyme Description: Pullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
943	MGYG000002836_5|CGC3	104632.45	4.4265

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002836	4582914	MAG	United States	North America

• Gene Location: Start: 167651; End: 170482 Strand: -

Full Sequence      

MHKRIKALFTVIILIVFTILGSYQPAYLVKAAQELTINVHYHRSGEDYEGWNIWSWLDGK
EGAAYEFTGEDKFGKVATYTLAVEDDTTQVGFIVRHSTSTNEWDMKDVESDRFIDIKKAK
NGIIDIYVVQDEIEFGYTQEDMSLAPKIKEAAIENSTTIDFKVSTAFDSTAADIKSKITV
KDADGKTYAIDKISSEKGKEALGARVTMSTELDLLKNYTLAFEGYGEMSISNTKVFSTAE
FEEAFTYEGNDLGAIWSKDKTAFRLWAPTASDVVLNLYSEGSGDNNIENIAMTKDVKGTW
VTEKPGDLDGVYYTYSVTVDGVTKEAVDPYARAAGVNGKRGMVIDLDSTDPDGFLQDEKP
ALVSPTDSIIYELHIRDFSIDKSSGMQNKGKYLAFTETGTKSSTGEKTGMDYLVDLGITH
VHLLPSFDYASVDESKPEDNQFNWGYDPENYNVPEGSYSTDPEHGEVRINEYKQMVQSLH
KSGIRVIMDVVYNHTSSSVDSNLNKVVPNYYYRMNEDGTFSNASACGNETASERAMVRKY
IVDSVVYWAKEYHVDGFRFDLMGIHDIQTMNEVRKALNEVDPTIVIYGEGWTAGGSPLPD
EEKALKANVSSLDAYIGAFSDDIRDGIKGSVFEDMDQGFVNGKTGMEETIKFGVVASTEN
SQIDYDLVNYSDTWWAKEPTQTINYASAHDNNTLWDKLAISNETDSEEDRIKMNLLSGAI
VLTSQGIPFFQAGEEFLRSKPSDDGTSFVDNSYNSPDSVNSLKWDTLTKNKEVFNYYKGL
IAFRKAHSALRMTKTADIQENLKFLEGLEPNVVGYTIDNSPNGETAKSLCVIYNSNKETS
AITIPEGDWNVYVKGQQAGTEILETVKGGTITVEPISTMVLVQEDKKADTPTDNADNGQT
QEANTSRSKDGQNNKVIVFATIGLTVAAVIAAAFLLTRKKKIK

Enzyme Prediction     

No EC number prediction in MGYG000002836_01056.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	410	735	9.5e-121	0.9965397923875432
CBM41	36	132	4.5e-20	0.9019607843137255

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	0.0	240	862	1	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	366	784	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	1.03e-158	234	888	51	696	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PLN02877	PLN02877	9.36e-152	176	845	138	923	alpha-amylase/limit dextrinase
TIGR02103	pullul_strch	1.32e-151	213	883	86	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]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJS18678.1	2.62e-307	34	941	152	1018
QEH70112.1	7.00e-302	33	943	139	1030
ADZ84640.1	1.28e-299	33	943	139	1030
AMC08554.1	7.41e-299	34	885	152	982
VCV21250.1	1.94e-284	241	885	10	652

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WAN_A	7.69e-207	39	883	9	921	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
6JEQ_A	8.36e-195	225	856	14	630	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	1.32e-193	225	856	14	630	Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
6JHH_A	1.32e-193	225	856	14	630	Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
7LSA_A	2.75e-170	232	882	44	712	ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	1.52e-209	34	884	20	843	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	4.22e-142	235	881	90	708	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	2.94e-94	213	770	169	796	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2ZL64	9.15e-86	36	824	230	1059	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	1.17e-85	36	824	252	1081	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 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
0.050060	0.947289	0.001462	0.000491	0.000326	0.000342

TMHMM  Annotations     

start	end
7	29
916	938