CAZyme Information: MGYG000002570_00944

Basic Information

• Species: Ruminococcus_E sp003526955
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Ruminococcus_E; Ruminococcus_E sp003526955
• CAZyme ID: MGYG000002570_00944
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1641	MGYG000002570_25|CGC1	177123.87	4.9226

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002570	2026568	MAG	China	Asia

• Gene Location: Start: 24; End: 4949 Strand: +

Full Sequence      

MNKHGMLKATSVAIALCTVMSSTTFAFSTVASAATVDTTEKVSASTTKSKDNFSWDNASV
YFLLTDRFRNGNTSNDHSYNRGLDQSGKVLSNIDDRATFHGGDFAGVTQSIEDGYFNNLG
VNAIWISAPYEQTHGYVVGSDGNPSYAHYSYHGYYVLDYTQTDANFGTAEEFETLVDTAH
EHGIRVIMDIVMNHSGYNSLYDMAEYGYGTVAPGWEDAYYPHQNINNKTYHSFIDYDTNA
EDWANWWGPDWIRCGVAGYTEGGGSDLTMSLAGLPDFKTEQASTVGLPKILQKKWSREGR
LDSETAKINNFFTKTGRNATVSNYLAGWLSEWVREYGVDGFRCDTAKHVEFASWKNLKNA
CVDALKEWRANNPDKPGADWDEDFWMTGECWDHGVNKDGYYTQGGFDSMINFSTQGGGLL
SAGRVKGTYDGFAKAINNDDSFNVLSYVSSHDSVLARGDLIGTGSGLLLCPGGIQIFYGD
ETNRPMVAGVPNDGNGGAGHSLRSDMNWDSMDTNVLEHWQKVGVFRNNHISVGAGSNTSL
ASTSGYAFARDYDKNGITDKVIGCIYANANTDVTISVGDTWSDGQYLVNAYDQSSAVVSN
GKVTFNSGKNGTILVEEPDGRPLMSVKGDAEFTGTQTVTVSLDKCEQAKCSVDGGNKFIV
KDGDTITIGNTAYDGDTITITLEAENEIGSSESKATFKKKVQGGSTAPVKTSSRLVVKTA
DGSAPYVYAWTGASNTLLGAWPGTQLTSKDDNGNYYVDLNTTEAYNVVLNTGKGGAQSSD
ISGITGDAIITVKNTAFSSYDLEIVETPASPLEQLKKEGREVKAMTSSDYTASSWTAVES
VMKSVDALVAQGSDADDDQVAAMITTLQNAKAKLQLNVPALGYAVKGKNTVSGVAAPASK
VTVTVNGTAYTTQADDVTGVFTVTTATLNASSKLTFKAERNSVSSAVGAYNMSSGDITSL
IVPTTASQATQPTTARPTQPTTVRPTQPTTVAPTTQSPTQGTNLNISSKSNYFSNANVTF
KKGDTVCLEYIVDSSMNLVNAEWTLTYDNTKLAVDKERSAKLMPYVTNEVTNIMDAKGTI
KSNFSEIQNLADFSGGKALARVYFNVIGTGDTTVDFNLKTLSVGYLDSNYNLKFKPVVRG
GVAQTDVTSTPGFENFTAKTSTKISATAEQTDEVTLNFVVPKTVSSPKCWDDGIYLAYSN
NYQLNSFTKIPLTKTTEYLTPDLKSTKLTNGTYALYSVSLTKEQAEAINKATYVVLTNKS
NTYRTYVSSKYNLLKAPSGTYSADYNTAKTSVADLNGYTFIMNGDVATGTSVDGFGTYTG
YWTKCTTINAVAPASAKWKNCWNQGVYLAYSNDYKLDSFTKIKMTRTSTYVDVDSKSTQL
VDGTYPVYTVTLTEDQVKAIDSSSYVIFENASGTYRTYINGKYSVMKAPAGTQYSSTYST
TKAKLADREKNTFVICDGVTTGTSIEGYGTFTGYWSTSEIEIVESTATLYCVFPNPAKSK
TAMNKGVYLAYGSSNSANGLTKIAMEKTDEKFTPSLKTNALTAGEYSVYKVTLNSDQIEA
IDGAKNVVFCNSNGVFRTVLSNGYNVLNAKSGAYSSAYNKGTFSVADHNSETFVVCDSKV
TGSSTDGYGMFLGYWDLGKAN

Enzyme Prediction     

No EC number prediction in MGYG000002570_00944.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	102	482	3.8e-142	0.9972222222222222

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	0.0	40	562	175	676	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	1.95e-45	59	529	4	344	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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	1.65e-41	58	515	1	398	Glycosidase [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	5.41e-39	60	478	2	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.
cd11352	AmyAc_5	1.19e-38	61	481	3	394	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCN30960.1	0.0	40	928	45	1030
QCT06045.1	6.37e-261	7	759	1	754
QCT06087.1	3.15e-214	14	829	12	812
CDM67955.1	1.76e-196	53	772	68	796
CDM67952.1	1.15e-190	53	777	74	807

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2B_A	3.82e-24	49	554	34	424	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A	5.84e-24	50	547	2	383	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
5A2A_A	5.84e-24	55	554	6	390	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
6SAO_A	9.27e-22	55	606	6	426	Structuraland functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]
1A47_A	4.61e-20	60	362	17	248	CGTASEFROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 IN COMPLEX WITH A MALTOHEXAOSE INHIBITOR [Thermoanaerobacterium thermosulfurigenes],1CIU_A Thermostable Cgtase From Thermoanaerobacterium Thermosulfurigenes Em1 At Ph 8.0. [Thermoanaerobacterium thermosulfurigenes]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	2.70e-118	53	562	184	669	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P21543	9.69e-23	52	604	741	1183	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
Q05884	1.80e-20	95	691	91	689	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
O30565	2.58e-19	60	195	33	154	Cyclomaltodextrin glucanotransferase OS=Brevibacillus brevis OX=1393 GN=cgt PE=3 SV=1
P26827	2.68e-19	60	362	44	275	Cyclomaltodextrin glucanotransferase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyA PE=1 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
0.000414	0.998683	0.000206	0.000286	0.000204	0.000178

TMHMM  Annotations     

start	end
12	34