CAZyme Information: MGYG000001795_00782

Basic Information

• Species: Amulumruptor caecigallinarius
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Amulumruptor; Amulumruptor caecigallinarius
• CAZyme ID: MGYG000001795_00782
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1606	MGYG000001795_3|CGC1	174217.68	4.8844

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001795	2604985	MAG	Denmark	Europe

• Gene Location: Start: 69710; End: 74530 Strand: -

Full Sequence      

MKNHKFDIRRKLAMLMSGIIAGASVYAAVNSGDASLSDLELRVDGRNILSGFSSSTTTYN
VDLDDASMLTMSAVPSASDATVAIDFNGVPMTNHSLASLDGGDNVITYTVRSGNATKTYT
VNIKTPQVVREEYFTWKNATIYFVLTDRFYNGDTSNDNSYHRRRLSGDADVATFHGGDLK
GLTQKLDYLDKLGVNAIWITAPYEQMHGWTGGKNDAFPHYAFHGYYALDWTYMDRNMGTI
EDMRNFVTEAHKRGIRVVMDIVMNHTGYCTLDDGVDYDFGNFNGTPTAGWVPSSTPYSMW
AESNQISFNANEQGNWGNWWGPWVRAFGDRSWATSAGYAPEGGDDYTKPLAGLPDIVTER
TAAVDIPPFLKKKWAAEKGGDYDLYRLPNLESWRTGSKGAPADYLVNWLAGWVEYFGIDG
FRCDTAKHLEKSRWNQLKTACKQALVNWRNSDRADEYAKDWDEDFWMTGEAFGWDHGDVG
YFTEGGFDSMINFAFNSSEGSQGRTPTTEEWKYYSNYCNGSNGRQVLNYVSSHDTGLHRP
GDQKKVATMLLLCPGGAQIYYGDETSRPYMSSSCGGDQSMITRSDFNWDAVDNADNKHWQ
IIGQFRRRNAAVGAGTQTDLGSDTYGRKFSEGAYSNAVVIKLNTSAGQTYTVSVGDHFAD
GAKVMDGYNTANTATVSGGKVTIAASGPVLLLEPYGTIGGGPGPQPVRPTVTANPPSGTT
FTESVTVTLMSTQGADIHYTTDGSTPSSSSATYSTPLTFTETTTLKTYVGNSNGSNIQTF
TYTKNSGGDVKPVVTASPAGGEFTGSVSVPLSVNPAGVPIHYSTSGTATASSPVYSSALT
FTETTTLSTYVENGAGSNTQSFTYTKQGGPDNTHYVYYDGTFSAPQVWAWVDGNTSCTTA
TAWPGDNMVKKDGKWYWEVPAGKPIPRMIIIHEGDNKIGGGDLTYVDKATYHQDGTYTPD
GGDDPEPSDVKVYYKGSWNPVNVYIYKAGAGEGAPANGAWPGVAMTKESGKDYWSYTVPE
NLKTGAKVIFNNGSDQYPQDVQGQECGLDLNGKSMMYDGGTGWSEFSEGPQKPSITITPN
GGTVKGSATITVVINNDATSISGTFNGSQLSLSNGSNSISVSRYLTSGGATGSLSVTATN
DVGTTTASASFTRDDSTPVYNLTGDWRELSIYQVMVGSFQHGDGGASGYSDMWGPEGHRK
NGNLRGIINALDYIKDLGMNAIWMTPIFDSTNGQGGEKLQATGYFCTNYFAVDPKFGTEA
EFDELVRKAHEKGIYIILDGVFGHHGGVSSASPNGNWISTQDNTPNVRGSESGNIQYPGS
LEYFKEVVRYWMERGVDGWRLDQCYQVYQGGHNYWKELREEVEKVASERKARGEQWGTLG
YMVGEDWTSAANITVTQQDGLKSVMDFDGKDNIVELGYGVGSIGWFLASDAAARGYRDSG
VNPTLFLSNHDTARVGDFVDVNSRPEELMTRHAAVAAYSGPTCTYYGDEIGDKSGNGNPD
NKARTSGRISGFNSNEQRVHDYVSKVFKARAANPALWRGTVSRQEGNKYEVITKTDAQTG
NKVVCIFSEIDTNVSIGGSGIDLINGGSVSGTVSVKAWIPAFIKLN

Enzyme Prediction     

EC	3.2.1.98	3.2.1.60	3.2.1.-	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	177	565	9.3e-122	0.9972222222222222
GH13	1199	1491	6.6e-80	0.98125
CBM26	971	1039	6.5e-18	0.8933333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	1.67e-163	134	625	185	663	alpha-amylase; Reviewed
cd11338	AmyAc_CMD	2.84e-54	1171	1539	4	387	Alpha amylase catalytic domain found in 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). 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.
cd11339	AmyAc_bac_CMD_like_2	2.75e-50	140	609	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.
cd11316	AmyAc_bac2_AmyA	1.29e-49	1172	1539	4	403	Alpha amylase catalytic domain found in 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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	6.92e-48	1171	1486	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SBU87531.1	2.73e-161	118	1045	27	937
BAF93484.1	7.35e-161	118	1045	27	937
BAB04132.1	1.02e-160	118	1045	27	937
BAG70894.1	3.83e-160	118	1045	27	937
AAS99099.1	1.45e-156	118	1045	27	937

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1J0H_A	8.54e-29	1165	1576	130	544	Crystalstructure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0H_B Crystal structure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0I_A Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus],1J0I_B Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus]
1J0J_A	2.01e-28	1165	1576	130	544	ChainA, neopullulanase [Geobacillus stearothermophilus],1J0J_B Chain B, neopullulanase [Geobacillus stearothermophilus],1J0K_A Chain A, neopullulanase [Geobacillus stearothermophilus],1J0K_B Chain B, neopullulanase [Geobacillus stearothermophilus]
4E2O_A	6.56e-28	135	564	6	328	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
1WZK_A	1.45e-27	1163	1548	124	512	ChainA, Alpha-amylase II [Thermoactinomyces vulgaris],1WZK_B Chain B, Alpha-amylase II [Thermoactinomyces vulgaris]
1WZM_A	2.56e-27	1163	1548	124	512	ChainA, Alpha-amylase II [Thermoactinomyces vulgaris],1WZM_B Chain B, Alpha-amylase II [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	2.74e-118	54	620	98	651	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
Q05884	4.45e-28	170	619	91	533	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P38940	4.68e-28	1165	1576	130	544	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
Q08751	3.30e-26	1163	1548	124	512	Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII PE=1 SV=1
A0A7U9P668	3.37e-26	1165	1566	130	533	Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 PE=1 SV=1

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
0.143890	0.846980	0.005004	0.003054	0.000613	0.000416

TMHMM  Annotations     

start	end
12	29