CAZyme Information: MGYG000001438_01690

Basic Information

• Species: Paenisporosarcina sp000411295
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_A; Planococcaceae; Paenisporosarcina; Paenisporosarcina sp000411295
• CAZyme ID: MGYG000001438_01690
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2280		251517.01	4.3804

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001438	3493887	Isolate	not provided	not provided

• Gene Location: Start: 1699100; End: 1705942 Strand: -

Full Sequence      

MRIAIDVKRKLNMFIVSVLVLSLWLPFIPAQQAHATSSTETGVNELTDSSNRHVRFTYIR
EDQNYGTWNIWAWNTGIKNDQINFESYEGGVASVNIAVAPEMKQFGFVLRSTDNWDTAQK
EFGDRFIQVNKNDSLTKAYITSGVEQIRIVPDGSAPVIDKGDATFYYRDKALFASDDMDT
IEKVELKFNGQTNEMTYEPENERFVFSYDNIPNGKTSYSFLVTKGGITTEVTDPYNTTDG
VSTIDFKKADLTVSGSVEPVAIDYNQNAVLTVDIQGLTDDVKISKISADASSLGGSANLE
IDPSLKEIAIAVDDDTTVGIKTIPLTVVDSYGNTYEGTAEVEVKTRQSTGTSDFDWDESV
IYFMLTDRFFDGDESNNDPYDLNYDTSKRGTYQGGDLKGITSKLDYLDDLGVNTIWISPI
VENIKYDVRSVETNGSSVDPYYGYHGYWASDFGKLNPHFGTMEDFHELIDAAHARDMKIM
VDVVVNHTGYGLKEIDGAMANKPAGFPTDEERANFSDIVRQGADVGTDEVVGELAGLPDI
KTEDPAVRQQIIDWQTSWIEQATTANGNTIDYFRVDTVKHVEDATWMKFKNALTDKKPEF
KMIGEAWGANVNNNLGYLNTGTMDSLLDFEFKNTARNFVNGQLKAANESLVDRNGKIDNA
ATLGQFLSSHDEDGFLHSLGGDEGKLKVAASLQATAKGQPVIYYGEELGLSGANNYPQYD
NRYNFVWDQVENNDVLEHYTKILNFRSEHSKVFAKGERTFVGGSDKDKFLLFSRDYQDQS
VYVGLNVAEEAKDVTLTVDSADAVVTDYYSGEVYEANEAGEINLSLPSKADGGTVLLTVE
DGNIIGAVATGDGNPEVEPIPDNTIRIHYNRQDNVYENYGAWLWNDVASPSANWPVGATM
FEKTDSYGAYIDVPLANGAKNIGFLVMDITKGDAGKDGGDKGFTISQPEMNEIWIKQGSD
KVYTYEPVNLPANTVRIHYTRENADYENLGIWNWGDTAAPSDGWPTGAVDLDGTDRYGAY
ADIELKEGAKDIGFLIVNQQTQEKDAGDKSFNLLDKYNHLWIKQGDNNVYISPYGEVASG
IVSGEVISEDTILLGFTMTDGLTSEKLKDDLAIKDVDGADVSIESIEITGATTVEVTATL
NLDKLPLSITYSGRTVSASTGWRMLDKLYAYDGNDLGATYKNGSATLKLWAPKASKVVAN
FFDKEDATAPIDTVELTLGEQGVWSKDINPSDLGVSDLNGYYYQYEVTNDGVMKTVLDPY
AKSMAAFTVNTEGDAGPDGDTVGKAAIVDLSGTNPKGFGHASIDGYEKREDAVIYEVHVR
DFTSDPSIEKDLKSRWGSYKGFIDKLDYIKSLGVTHVQLLPVMAWYYGDETKMGERELDY
SAGGNEYNWGYDPHSYFSPDGAYSENPKDAELRVKELKELIDAIHDADMGVVFDVVYTHM
AKASMLNDIVPNYYAYQDAKGNFLGGFGNNLATSHTMAEKLMVDSVKYWFDEYKIDGMRF
DMMGDATYSSIQKAYDVAASVNPDALFIGEGWRTFAGHLADPALAGMGADQDWMDKTDDV
GVFSDEIRNELKSGFGSEGEPRFITGGARNIDTIFNNIKGQPSNTADDDPGDMVQYIEAH
DNLPLYDVIAQSIKKDPAIPENDLEIHKRIRIGNSLILTSQGTAFLHAGQEYGRTKQWLG
EGVPEQKYHELKDMDGNTFGYFVHDSYDSSDAINKFDWQKATNKKEFAVNTTTNAYTKGL
IDLRKSTNAFRLGEKALVDTNVSLLDFPEMKDSDLVIAYENISTDKTGNYYVFVNADNKA
RTLTLGDYDFTGGVVLVDNDEAGTHPVSKKSGFSLSNQTMTIDPLTTVVIKLDRKATEEP
KNNGNDGYQPPANGKPNTIVLPPQAAEVVKEKNPSGMIEVVTKIIPGKVSEIVNAITPEK
FVVALKLEKPATGETVKVQVPGSLFKEALKKNKQAMIEIQTDEATYKLPASEINVADLAK
KLGVAESDVQITVSVNVVKSPSTKAKIVSNTIEFHVEAVAGDKKVTITAYGSFVEREIVG
DKEFNPKTMVAVKFNQDGTFTSLPTVFNGKIATVKSLTNSTYAIVENNQIFPDVNNINWA
EDSIEKLASKYIIKGKADGTYAPAEEISRAEFTVLLVRALGLPAKAYDKRFSDVKGTEWF
NANGELMAAVQYGIINGKHDGTFAPYEKLTRTQAAVMISRAMELKFLNFDFAKLDHAKKL
ADFKDANQMTDWSRVGIENVYQAGIMDGKSNGTFDPNGFTKRDQMAKILARFLEVSNLMN

Enzyme Prediction     

EC	3.2.1.41	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	395	713	5.1e-117	0.9931972789115646
GH13	1337	1675	2.1e-109	0.9964788732394366
CBM41	863	967	3.9e-31	0.9901960784313726
CBM41	973	1074	6.2e-29	0.9901960784313726

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02102	pullulan_Gpos	0.0	860	1906	1	1051	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 (.
cd11341	AmyAc_Pullulanase_LD-like	1.09e-141	1310	1744	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	6.18e-139	1168	1803	60	640	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02104	pulA_typeI	1.14e-136	1166	1826	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.
cd11339	AmyAc_bac_CMD_like_2	3.12e-81	358	712	2	299	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AGX06343.1	0.0	8	2280	5	2273
ANU15501.1	0.0	8	1861	6	1845
ANU24793.1	0.0	8	1861	6	1845
QWC22460.1	0.0	8	1862	6	1860
QTC40332.1	0.0	8	1855	6	1853

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2YA1_A	9.33e-258	862	1854	6	1013	Productcomplex of a multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
2YA0_A	3.06e-209	1162	1857	2	709	CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
2YA2_A	1.30e-208	1160	1854	1	707	CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA in complex with an inhibitor. [Streptococcus pneumoniae TIGR4]
3FAW_A	8.68e-207	1048	1856	7	817	CrystalStructure of the Group B Streptococcus Pullulanase SAP [Streptococcus agalactiae COH1],3FAX_A The crystal structure of GBS pullulanase SAP in complex with maltotetraose [Streptococcus agalactiae COH1]
2WAN_A	9.20e-81	867	1851	9	920	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0A0H2UNG0	2.41e-256	858	1857	131	1145	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64	3.21e-256	858	1894	116	1158	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	1.57e-255	858	1857	138	1152	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
O33840	1.27e-80	974	1850	22	840	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	3.72e-67	1166	1790	97	654	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX 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
0.000500	0.998711	0.000182	0.000234	0.000174	0.000160

TMHMM  Annotations     

start	end
13	30