CAZyme Information: MGYG000003569_01012

Basic Information

• Species: Treponema_D sp900769975
• Lineage: Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900769975
• CAZyme ID: MGYG000003569_01012
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1274	MGYG000003569_93|CGC2	146447.52	6.6434

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003569	3076540	MAG	Fiji	Oceania

• Gene Location: Start: 25264; End: 29088 Strand: +

Full Sequence      

MQISYNEFHISKKVRTLCNFNKGLFASSGNVVFANMKNVRDFQLLFNDYIEQTTGDKNKK
VSAGQLNAMGLIDEILHYVCFVYRRDKVNDFSKELLAKLDNEYGVQKIDSLLLDFMNEFP
PVEVYQEKCTAQEYLSRNAVDSGTMTERSNREQTLEELILLHLANENPAFKPFALLFDDS
VLQENNELYSKTWAFIQKYAKTKPVFGPFNHDLITMMREPVTFSPESLKGQLEYIQKYWD
KLLGEWLKRILSGMDAITEEEKAMWHGFGGGDLPDMVPYSFENLMNEYERFSPDSEWMPN
VILMAKTVLVWLDQLTKQYGYPITKLDQIPDAELDKLRDEGFTGLWLIGLWERSKASKRI
KQICGNPEAAASAYSLYDYNIAANIGGWDALANLRQRLWQRGIRLASDMVPNHTGMDSDW
VMNHPDRFIQRRDNPFPQYTYSGENLSHDSRTSVYLEDHYYSKDDCAVVFKRVDNQTGDV
RYIYHGNDGTGLPWNDTAQIDFLNPEAREAVMQEILHVARNFPIIRFDAAMVLAKKSIRR
LWYPEPGHGGDIATRSETGLSTQQFNDAIPNEFWREVVDRVAKECPDTLLLAEAFWMMEG
YFVRTLGMHRVYNSAFMNMLKKEENQKYRDTIKNTINFDPQILKRYVNFMNNPDEETAIA
QFGDSDKYFGVCTLMVTMPGLPMFGHGQIEGFTEKYGMEYTKAYKDEKPSQYLVDRHWHD
IFPLMKKRYLFSGVENFLLYDLWENGHVNENVFAYSNGAGSERTVVFYNNKYDRACGWIK
QSDPYAIKTGNGDEIKLVTKSLSEGLGLSADDDRYCIFQEHRSRLWFIRKNSEICEKGMF
VMLNGFEYQVLLNIQEVKDEADGRYRILCETLAGKGCEDIESAWQEIIYKDLYKDLEVFA
DEAIIPIVKEFDESSAISKTDEKGDALSKTPCKDSAGETKDDGNASNSTNDTNNSTDATS
SLSASKISWTKINKIITNAKNSAIKFYETAKRFSLEDASIKTPAEPEKQFALFKNSIKQL
VELHNAQPLPSPENLQKTLEKTAGSTAEINDFIKLLMQSNEKLEYILVANAVCAEYSQNT
LADKWNLARKLNSYMKKDLTYDFKKAFKLIPLADSSKLPKDEKKVACKIVDFLVRGRFAK
NLSGANYFDNTLWFNKELLEENLNLVFVFMLLNSQKSKIPAVFDLYKTVCEAKDKAEYKA
ELFVKQFEPLKKAEKSAKQKGKPNTTKIANGAKASKVVKTAKFSKETKTPDAKKQQQKKN
LKQKKADSKKKQKK

Enzyme Prediction     

No EC number prediction in MGYG000003569_01012.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	332	694	2.2e-21	0.903010033444816

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11347	AmyAc_1	1.22e-61	310	695	10	351	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.
cd00551	AmyAc_family	6.19e-18	334	686	31	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.
cd11313	AmyAc_arch_bac_AmyA	9.28e-17	332	701	26	299	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.
COG0366	AmyA	1.41e-06	334	682	35	348	Glycosidase [Carbohydrate transport and metabolism].
smart00642	Aamy	2.14e-06	333	428	24	114	Alpha-amylase domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNL98042.1	0.0	1	1228	1	1180
QQA01503.1	0.0	1	1227	1	1195
AEB13435.1	0.0	1	1225	1	1190
QTQ13027.1	0.0	1	1220	5	1262
QTQ15274.1	0.0	1	1220	5	1273

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000069	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003569_01012.