CAZyme Information: MGYG000000479_00179

Basic Information

• Species: Treponema_D sp900541995
• Lineage: Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900541995
• CAZyme ID: MGYG000000479_00179
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1218	MGYG000000479_1|CGC4	138860.71	6.5983

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000479	2347794	MAG	Fiji	Oceania

• Gene Location: Start: 198390; End: 202046 Strand: +

Full Sequence      

MNKSYNEFHISRKVRKECAFSESMFSSSGNVIFANLKAVQEFQTKLNSLFDKNGEPQKKV
SAGSLNAMGLIDEIFHYVCMIFRRDKAPDSFKNLLEDLDTYFGSEKVNDLLLEFMEQFPP
VAVYRNEITAQDYLSQTCMDEGTKKPRTNREQVLEELVLLHLANENPAFHPFQILFDDTE
LSKNADYIKTWNQIKAFFLTQPVFGPKNNDLISMLKEPVVASPTSLKGQLDYIRTHWAAL
LGEWLIKLLLAGMDTISEEEKAAWHPTNGGSPDMAPYSYDNLMKEYERFSPDREWMPKVV
LMAKTVLVWLYQLSKKYNRDINRLDQIPDEELDALRDEGFTGLWLIGLWERSYASKRIKQ
INGNPEAAASAYSLLDYEIASNLGGWPALENLRYRCWVRGIRLASDMVPNHTGMDGKWVI
EHPDLFITTKECPFPSYTFNGENLSQDSRVSIYLEDHYYSKSDCAVCFKRVDNQTGDVTY
IYHGNDGTGMPWNDTAQIDFLNPEAREAVMQQILKVARNFPIIRFDAAMVLAKKHIRRLW
YPEPGHGGDIASRSRYALSSQEFEARIPNEFWREVVDRCAAEMPDTLLLAEAFWMMEGYF
TRTLGMHRVYNSAFMNMLKKEENQKYRDTIKNTIKFDPQILKRFVNFMNNPDEETAVAQF
GRGDKYFGVCTLMITMPGLPMFGHGQLEGFEEKYGMEYTRAYKDEQPDEGLMQRHRHDIF
PLLHKRYLFAQIENFLFYDVWNNGSVNENIFAYSNSVGNERTIVFYNNKYERASGWIKQS
CEYAVKTGPGESDVRTESKSLSEAMGLTYGQNHFCIFREHKAGLWFVRKSDDIINGGMFV
GLNGFEYQVYLDVQQVEDTADGKYAKLNELLNGSGTKDLDAAWLEYRYKELYASLKKFLT
AEFISALREIFASDTEDGSKKKKKATAKTVCEAVKEAALEYYTLEAEFASKEISADDTTA
SQKKTRKTAKITETTAEQRFDAFCKQVEFLAKAVKPVAKDKASDKTTEANTAFADLIKEG
LNLYKDAPAIIVASAAVLSAGNENCLKWGYTRKLAEILSKTGTDENYASNILERIFTFTG
IRDMNFAASGFVKSTYETAKLLALSEHSGLLSGANEFGGTKWFNKERMEETLWYGTTVLI
TASAKILREQMFRLYRTLSAALEKSEYKCENFVESVKPKKVAKVTTKKASPAKTKAAGKT
KSAGSALASKKSSKDSKN

Enzyme Prediction     

No EC number prediction in MGYG000000479_00179.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	323	692	7.9e-20	0.9163879598662207

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11347	AmyAc_1	8.24e-57	308	711	10	368	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	1.77e-17	330	684	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.
cd11313	AmyAc_arch_bac_AmyA	9.19e-17	330	701	26	301	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.
pfam00128	Alpha-amylase	2.47e-06	330	690	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.
COG0366	AmyA	1.34e-05	332	680	35	348	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QQA01503.1	0.0	1	1218	1	1218
AEB13435.1	0.0	1	1189	1	1184
QOS40801.1	0.0	1	1197	1	1159
QNL98042.1	0.0	1	1183	1	1167
QSI03061.1	0.0	1	1183	1	1200

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
1.000064	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000479_00179.