CAZyme Information: MGYG000003457_00292

Basic Information

• Species: UBA9732 sp001940825
• Lineage: Bacteria; Spirochaetota; Spirochaetia; Sphaerochaetales; Sphaerochaetaceae; UBA9732; UBA9732 sp001940825
• CAZyme ID: MGYG000003457_00292
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1095		126610.03	5.11

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003457	1983561	MAG	Fiji	Oceania

• Gene Location: Start: 64054; End: 67341 Strand: +

Full Sequence      

MKNRDLRISEPSRIEMSYESPVFETSSKIGVMYRQAQELTHIYNESHDRPLSAANVHICA
VLHLIYQTVISAYLKGTDSDPFSRIQVLAQKNEACKEVLGFYNRMFPTKLTDQRFDGLDE
TARAFFVHQVFESNPAFLTATGNMFDQSTMVFPQGTKALTGMMGSYLKGTSFIENTDSDD
LFSFLTMPSRLFPDSLMKQMEYITEHWDMLLPEELNTLLLKAKDYLREETKPHPMGPGPG
PMEIPSFKDEDQDFERFTPDKNWMPNVVMMAKSTLVWLDQLSKKYERDISRLDQIPDEEL
DYLRDSGFTALWLIGLWERSPASKKIKVLCGNPDAESSAYSLKGYEISSRIGGWQSLYDL
KKRCWERGIRLASDMVPNHTGIDSDWMMEHSDYFIQQSYPPFPSYTYNGPNLSDNPDIDI
RIEDHYYDRTDAAVTFRRVDRRTGETSYIFHGNDGTTMPWNDTAQLDFLNPTTREAVIQQ
ILEVARNFPVIRFDAAMTLAKRHIQRLWYPKPGTGGDIAGRIPYEMTDEEFNRRIPNEFW
REVVDRISQELPDTLLIAEAFWMMESYFVRTLGMHRVYNSAFMHMIKNQDNAKYREMIKS
TIAFDPEILKRYVNFMNNPDEDTAIAQFGDTDKYFGACTLLSTMPGLPMFGHGQIEGFRE
KYGMEYQRAYWDEKPDERLIAEHRRRIFPLLKMRRLFSESKNFQLFDVHREDGSTAESVF
AYVNGDDNQMALVLYNNQYDHVDGTITESAPKLVRNGEEKSLETVSLAKSLRLTRGVRRY
VIYRNFNDGLYRIMPSVKLYEEGLKVSLNGYETMVVTNIYEIEDIDGIYQKLYEKMGSRG
MESIEHEMQILYLGPFFEAVDPIRSQKFAKDLRTILNGTSTSANKKGIMQTLGTCYTYMD
ELTGLFEKIGLHPRRMKAQVILDMVNTLEAICRRKPFQNANLILDDMLATVVSAALLEMP
FINPDGTGLAESFEIARTLQLDRLFGVQPSVAFRCAILNASKPKEMEELLCNKTFQMLIG
CNEYQGVRWYRGEAFQECMYLNVLSQAMQCMDKGADKGVDADECTKESEKELRKWLDRSN
QAQYRLDNLMEGTHC

Enzyme Prediction     

No EC number prediction in MGYG000003457_00292.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	294	660	1.6e-23	0.9163879598662207

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11347	AmyAc_1	5.35e-63	273	692	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	1.10e-21	298	695	26	328	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	1.14e-18	298	652	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	2.32e-10	300	648	35	348	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	1.01e-09	298	658	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	16	1048	1	1070
AEV29686.1	0.0	4	1045	4	1085
AEC03027.1	0.0	4	1053	31	1118
ADK79422.1	3.22e-285	181	1091	195	1128
AFG36209.1	8.90e-285	132	855	160	881

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2TAA_A	5.66e-06	298	410	47	148	StructureAnd Possible Catalytic Residues Of Taka-amylase A [Aspergillus oryzae],2TAA_B Structure And Possible Catalytic Residues Of Taka-amylase A [Aspergillus oryzae],2TAA_C Structure And Possible Catalytic Residues Of Taka-amylase A [Aspergillus oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P07190	2.24e-06	298	676	52	412	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
1.000023	0.000013	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003457_00292.