CAZyme Information: MGYG000000902_03645

Basic Information

• Species: Clostridium neonatale
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium neonatale
• CAZyme ID: MGYG000000902_03645
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1598		177104.15	4.3508

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000902	4770522	MAG	China	Asia

• Gene Location: Start: 663; End: 5459 Strand: +

Full Sequence      

MGKIRKRIKSIIAMTLVVTTIITSGLNFKIVANAETVNNTVTSNYGLAGNTEDGVILHAW
DWSFNTVKDNLEDIAKAGYTSVQVSPIQPSKNDNYTTNSKWYILYQPIAFEIGNKQLGTE
EEFKAMCDEADKYGIKIIVDVVANHTGNNEGDGNTTIAPQVKFQGAGFEDYWHNPLHGVT
DWDDRKEVTHGGIGLPDLNTSNKDVQKMVRNYLEECLKDGADGFRFDAAKHIELPTDKEG
ISSDFWPSVLDGLKTTDGTNPYIYGEVLQGGADNYAEYTKIMHVTTSNYGNNIRKAVGLG
TSANVSNAIDYDVPPEVNPSRLVTWVESHDTYANDSEESTGMTSEQIKDGWAIIAARADS
TPLYFNRTAGRKKLQGNIGDAGNDDWKDPDVVAVNKFHNDMADEDENLVKVSKEILMIER
GNKGVVIVNLANDCSINQDINLEDGIYNNCATSGGTFSVKGGKISGTLSKGITVLYKDGV
PEKPSTSPKVSISEEDCSFEGTLDLTLNVTNSTNATYSINNGQEIVYTNGQQITIGQDAE
AGDKIKVVVKAVNEDRKASEEYNYIKKDSNSVATLYFRKPDGWMAPYVYIYNELDEEDCA
WPGNKMTKIDDDLYKYELKGFTDSKVMFNDWFYGGNKTEELDLTATGKMLYDSSKSDKWS
ATEDIEANPNVKPDVEEKSTSKVYLKKPADWEKDDIYIYFYKNGASGPAWPGIPMEKVEG
KDDLYTYTLPKGLEGAMVLFNCDGGSVQVPKDTGFKAPANTTMIYDESWKEYTENSSKVY
FRKPAEWGEPNVYAYKSSGGENEKWPGAKMEKVSATETLYSYTLPENFGDCNVIFNDGSN
KYPSKEGYALSVGDVKIYDNDGLRDFTLDDLEEPEQPSDDEEQGVTKVYFENTFGWDKVK
VYAYNDGTSDEVKAWPGVNAKDEGDNLYSYTLPNGFESATVIFNNGSGGEGNQTGNLKTE
AGHTMIYDAENDVLKSLSKVYFKNTEKWDKVKVHYWIDGGASTNWPGMSMTYEGDDLYSY
TLPDDFQNVNVIFNNNSNGMQSETVKIKEGETLIFIPSLTGSEDNREGQWRAFEKSDIPN
SSTNPDPDEPDTDEEVGSTVYVKLPEGWSGIPNMHYWNAVGGQTEWPGKAMKDEGNGIYS
CEIPKSFGDVSIIINDGNNKLTDSEGNNEFAVKLGSSIIFEDGVWRDYVKPNPGPEDPDD
GDDDNKEVSKAPKVNGDIYTTTTNVIGTAGANAEMILTVDEIVETTTSDGVTLKTIKDVE
KKEIGSAKADENGRWSANISKQEKGTVITITATEEDKEPASIEVTVKKKSSSSSSGSTSS
SSSKKKTSKPITISRVEDALSNAIKGNINIDSKKPYIEKDVFDFLAKNPNKTITLIGNGY
SWTFKGSDINSSMVLSEDIVTTISNVSPKQESINKLAKGNDILTLHFDYEGLLPGKASVQ
INVDSKYNDSIMNLYIYNEKLNKLELLSENIEVKNNNINIEVLRGADYILSKTKIPGVIK
SGWNLNENNAWIFIENSDLVKGWKLVDNKWYLMDANGIMRTGWNLINSKWYYLNESGAME
TGWLCINDKWYYLADNGVMLSNTTINGYILGNDGVWIK

Enzyme Prediction     

No EC number prediction in MGYG000000902_03645.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	62	336	2.5e-98	0.9924812030075187
CBM26	887	956	1.4e-17	0.8933333333333333
CBM26	979	1040	6.5e-17	0.8666666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11315	AmyAc_bac1_AmyA	1.14e-146	53	408	1	352	Alpha amylase catalytic domain found in 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, Proteobacteria, Actinobacteria, and Cyanobacteria. 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.
cd11317	AmyAc_bac_euk_AmyA	1.13e-38	54	352	2	256	Alpha amylase catalytic domain found in bacterial and eukaryotic 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 AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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.
cd11320	AmyAc_AmyMalt_CGTase_like	6.13e-22	69	330	51	313	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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.
cd11319	AmyAc_euk_AmyA	1.25e-20	63	330	41	297	Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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.
NF033840	PspC_relate_1	2.90e-20	1497	1598	526	648	PspC-related protein choline-binding protein 1. Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCJ05706.1	0.0	4	1216	2	1238
QSX02258.1	0.0	4	1216	2	1238
QJU43232.1	0.0	4	1216	2	1238
QUF82755.1	0.0	4	1216	2	1238
BBK77894.1	0.0	4	1216	2	1238

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DC0_A	3.20e-105	52	478	4	422	Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1UA7_A	1.42e-103	52	478	4	422	ChainA, Alpha-amylase [Bacillus subtilis]
1BAG_A	2.93e-103	48	478	3	425	ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
1G94_A	3.08e-17	57	330	6	264	CRYSTALSTRUCTURE ANALYSIS OF THE TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS IN COMPLEX WITH A HEPTA-SACCHARIDE AND A TRIS MOLECULE [Pseudoalteromonas haloplanktis],1G9H_A TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA-AMYLASE, COMII (PSEUDO TRI-SACCHARIDE FROM BAYER) AND TRIS (2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL) [Pseudoalteromonas haloplanktis],1L0P_A Crystal Structure Analysis Of The Complex Between Psychrophilic Alpha Amylase From Pseudoalteromonas Haloplanctis And Nitrate [Pseudoalteromonas haloplanktis]
1JD7_A	3.19e-17	57	330	6	264	ChainA, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00691	1.23e-126	32	630	31	627	Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P23671	2.99e-95	1	495	1	477	Alpha-amylase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=amyA PE=3 SV=2
P30269	2.87e-82	53	812	147	970	Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
Q23835	4.59e-25	31	366	15	346	Alpha-amylase 1 OS=Drosophila ananassae OX=7217 GN=Amy35 PE=3 SV=3
O18345	6.13e-25	31	366	15	346	Alpha-amylase 2 OS=Drosophila ananassae OX=7217 GN=Amy58 PE=3 SV=2

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
0.000722	0.998223	0.000373	0.000276	0.000190	0.000175

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000902_03645.