CAZyme Information: MGYG000003642_00220

Basic Information

• Species: RUG572 sp900771305
• Lineage: Bacteria; Verrucomicrobiota; Kiritimatiellae; RFP12; UBA1067; RUG572; RUG572 sp900771305
• CAZyme ID: MGYG000003642_00220
• CAZy Family: GH13
• CAZyme Description: Neopullulanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
477		54028.65	8.2716

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003642	3810265	MAG	Fiji	Oceania

• Gene Location: Start: 8773; End: 10206 Strand: -

Full Sequence      

MRRWMLMAALLFAAGAFGANAWMQNARKSPKWFTEGVMYQIQPRSFTPEGTLRAATRKLP
YLKDLGVTIAYLVPVMKMDDSRDKAFWSPRQIRSGFDNPKNQYRIADYFHVDEEYGTDED
LKDFCREAHRLGLKVVFDLVYFHCGPTAPFLREHPEFTWWNADGTVKKGPWRFPKLNFAV
PALRTYLIGNITYLMRTFGADGFRCDVGDGIPLDFWCDAHDAMDALRPGEAVLLCEGFTV
CDQYKGFDADYGWFPGLSAKTVRSAWIGRERQCPVGSRFVNHYENHDIATDARPRREKAW
GFDAVNQVITWMFTLDGVPLLFCGNELADADERHSMFGKTPMDWSQLDRAPGRARHALVK
ELARLRREHPALTAVNGRDGLIWLDTTKPDAVSAFARRGGGETLLVVQNWTGREVSCDVS
FAAPKESVPSYIVAENVDRDVKGAVDPAPLHARRAKHTAPRGFTLGPWGCWVSCVKK

Enzyme Prediction     

No EC number prediction in MGYG000003642_00220.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	42	328	6.3e-42	0.9464882943143813

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11313	AmyAc_arch_bac_AmyA	9.64e-77	32	372	1	333	Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes firmicutes, bacteroidetes, and proteobacteria. 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.
cd11338	AmyAc_CMD	4.50e-44	50	372	53	384	Alpha amylase catalytic domain found in 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). 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.
COG0366	AmyA	8.44e-29	36	416	1	489	Glycosidase [Carbohydrate transport and metabolism].
cd11350	AmyAc_4	1.12e-28	37	372	17	386	Alpha amylase catalytic domain found in an uncharacterized protein family. 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 (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.
pfam00128	Alpha-amylase	9.90e-27	50	327	1	326	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNN21909.1	1.39e-113	24	447	29	461
AVM44639.1	1.74e-107	25	414	5	405
QEH35363.1	1.57e-60	26	469	45	475
QKG72449.1	5.26e-56	19	469	29	458
QPC98033.1	1.01e-54	19	468	30	458

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	5.56e-33	37	342	14	328	Crystalstructure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_B Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_C Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_D Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum]
4GKL_A	6.51e-27	37	440	7	394	Crystalstructure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana],4GKL_B Crystal structure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana]
5OT1_A	1.47e-25	50	410	349	722	ChainA, Pullulanase type II, GH13 family [Thermococcus kodakarensis]
1SMA_A	6.14e-24	28	409	127	536	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]
1GVI_A	6.14e-24	28	409	127	536	Thermusmaltogenic amylase in complex with beta-CD [Thermus sp.],1GVI_B Thermus maltogenic amylase in complex with beta-CD [Thermus sp.]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
L8B068	2.03e-26	18	410	230	612	Alpha-amylase MalA OS=Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1) OX=1227453 GN=malA PE=1 SV=1
A0A7U9P668	1.45e-22	28	409	127	536	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 PE=1 SV=1
P38940	1.94e-22	28	423	127	550	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
Q08341	3.63e-19	24	452	122	584	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
Q9RX51	4.94e-19	37	206	128	275	Malto-oligosyltrehalose trehalohydrolase OS=Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) OX=243230 GN=treZ 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
0.098902	0.896933	0.002492	0.000764	0.000466	0.000416

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003642_00220.