CAZyme Information: MGYG000000677_01585

Basic Information

• Lineage: Bacteria; Spirochaetota; Spirochaetia; Sphaerochaetales; Sphaerochaetaceae; UBA5920
• CAZyme ID: MGYG000000677_01585
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1044		119848.59	5.1436

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000677	2015211	MAG	Kazakhstan	Asia

• Gene Location: Start: 2282; End: 5416 Strand: -

Full Sequence      

MLSFYLSDGQSDFFSRRVKTINENEDLKKALDFFTVNYPSIVLEENKTMGFEAETENMRG
YFIFQVMLNNPALISAAKPLITPDELTLPRSFKALSSILSSFEKDDLRDGEPNKDDIFTL
LSLPSRLYPNSLESQIKYMLREWSFMLPSELKRMLENSLDFIKEEEKDHGFGGAPGPMPV
ADYSEEAYEYEAFSLDSNWMPRVVMIAKSTLVWLDQLSKKYKRSITTLDQIPDEELDLLK
ERGFTALWLIGLWQRSEASKRIKHLCGNPEAEASAYSLKDYDISDKIGGWQALDNLRERA
NQRGIRLASDMVPNHTGLDSNWVYDHPEYYISQDYSPFPSYTYNGPDLSDNPNFEIKLED
HYYDRTDAAVTFRLTDKRNGKVRYVFHGNDGTTMPWNDTAQLDFLNPATREAVIQKIIHV
ARCFPIIRFDAAMTLAKRHIERLWYPKPGTGGDIAGRAEHSLSVQEFNKRIPEEFWREVV
DRIAVEVPDTLLLAEAFWMMEGYFVRTLGMHRVYNSAFMNMLKNQENQKYRQSIKNTLEF
EPEILKRYVNFMNNPDEDTAIAQFGDGDRYFSIATILATLPGLPMIGHGQIEGYREKYGM
EYSKAYYDESPNERLISEHYRRIFPLFRKRYLFSGVEHFNLYDCMNNGNVQEAVFAYVNG
SGAERNLVIVNNQYERSSGVINKSANKIVRKGDKKVIESISLAENLSLHFSAKNYVIFDC
FTDGLSYLYPSMNIFDYGFNISLNGYESKVYWNIREVEDTDGIYEKLYSIYKDKGIKNIN
KAIMLLKLAPIYKILEPLRRPDYLKLIDEIIKGKSTRETERSALLTLAEVYTTLYESYPS
MDESAKGLLDVPPYDVKPAPIVNIIKATAKLFSAKGSKAMRSWSSVDESVPLLCAIALTI
LPFSKGLDIKGTMEISDRLLISDFFENAMKSAGYYKEDEMRALAHEGALLLSAYSLSLLK
PEDILRAVLNDSGVMNLTKCNEYKGEIWFNKERMQKTILIASFAKAIEGNVPTELLDEEI
AILLEKEMKSGYKLNTLLAKNSVD

Enzyme Prediction     

No EC number prediction in MGYG000000677_01585.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	228	593	1.4e-23	0.9130434782608695

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11347	AmyAc_1	2.48e-68	209	628	7	380	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 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.
cd11313	AmyAc_arch_bac_AmyA	3.54e-22	234	626	26	326	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.
cd00551	AmyAc_family	1.56e-18	234	588	29	253	Alpha amylase catalytic domain 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; and 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 this 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	2.08e-13	236	584	35	348	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	1.16e-09	234	594	8	328	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
ADY11875.1	0.0	1	1038	59	1099
AEV29686.1	0.0	1	1039	74	1118
AEC03027.1	0.0	1	1039	99	1146
ADK79422.1	3.04e-277	112	996	190	1088
AFG36209.1	3.24e-276	70	848	162	938

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1QHO_A	6.51e-06	234	391	56	224	FIVE-DOMAINALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE/ACARBOSE COMPLEX [Geobacillus stearothermophilus],1QHP_A Five-Domain Alpha-Amylase From Bacillus Stearothermophilus, Maltose Complex [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P14899	1.44e-09	234	604	61	358	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
P07190	3.10e-07	234	590	52	396	Maltase A1 OS=Drosophila melanogaster OX=7227 GN=Mal-A1 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000077	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000677_01585.