CAZyme Information: MGYG000003177_01255

Basic Information

• Species: Amulumruptor sp900539915
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Amulumruptor; Amulumruptor sp900539915
• CAZyme ID: MGYG000003177_01255
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1501	MGYG000003177_24|CGC1	163812.46	5.5064

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003177	2162791	MAG	United States	North America

• Gene Location: Start: 5438; End: 9943 Strand: -

Full Sequence      

MKNHKFTIRRKLAMLMSGIIAGASVYAAVNSGDASLSDLELRVDGRNILSGFSSSTTTYN
VELEDVSMLTMSAVPSASDATVAIDFNGAPMTNHSLANLDGGDNVITYTVRSGNSTKTYT
VNIKTPQVVRDEYFTWKNANIYFVLTDRFYNGDTSNDNSYHRKRLSGDADVATFHGGDIK
GLTQKLDYLDKLGVNAIWITAPYEQMHGWTGGKNDAFPHYAFHGYYALDWTYMDRNMGTI
QDMKDFVTEAHKRGIRVVMDIVMNHTGYSTLDDGVDYDFGNFNGTPQAGWVPSGKPYSMW
SESNEISFNADEQGKWGNWWGPWVRAFGDRSWAPNAGFAPEGGSDYTKPLAGLPDIVTER
TSPVEIPPFLKMKWAAEKGGEYDNYRLPNLEGWRTDSKGAPADYLINWLAGWVEYFGIDG
FRCDTAKHLEKSRWNQLKNACNQALNNWRNSDRADEYAMGWDEDFWMTGEAFGWDHGDVG
YFTEGGFDSMINFAFNSSEGSQGRTPSTSDWKYYANYCNSPNGRQVLNYVSSHDTGLHRP
GDQKKVATMLLLCPGGAQIYYGDETSRPYMSSNCGGDQSMITRSDFNWDAVDNADNKHWQ
TIGQFRRRNAAVGAGTQTDLGSDTYGRKFSEGEYSNAVVIKLNTSAGQTYTVSVGDHFAD
GTKVMDGYNTANTATVTGGKVTIAASGPVLLLEPYGTIQQGSNPQPVKPTVIANPPSGST
FTESVTVTLRSTQGADIHYTVDGSTPSESSDTYSAPLTFTQTTTLKTYVSNANGSNVQTF
TYTKGQAPKPVVTASPAGGEFEGSVSVTLSVNPVGTPIHYSTSGTATASSPVYSSALTFT
ETTTLSTYVENAAGSNVQSFTYTMKPGGVDEHYVYYDGTFSAPQVWAWIDGNTNCTTAGK
WPGDNMTKKNGKWYWAVPSGKSLPKQIIIHEGDNRIGGGDLNYVDKATYHQDGSYTSKVD
DPTPQKPSVTINPNGGTVKGSATITVVINNDATSISGTFNGKSLSLQNGSNSVSVSQYLT
SDKATGSLSVSATNAQGTTTANVSFTRDDSTPVYEDNLTGDWRELSIYQVMVGSFQHGDG
GASGYSDMWGPGGHRKNGNLRGIIDALDYIKDLGMNAIWMTPIFDSTNGQGGEKLQATGY
FCTNYFKVDPKFGTEAEFDELVRKAHEKGIYIILDGVFGHHGGVNSASPNGKWIDSTTAN
NVRGTDAGNISYPGSLEYFKEVVRYWMNKGVDGWRLDQCYQVYQGGHNYWKDLREEVERV
AQERRSRGEKWGTLGYMVGEDWTGAGSITVTKQDGLKSVMDFDGKDNLVKLKNGVRSIGW
FLASDAAGRGYRDSGVNPTIFLSNHDTSRVGDFADVNSRTNELITRHAAVAAYSGPTCTY
YGDEIGDKSGNGNADNKARTSGRISGFNQNEQKVHDYTAKYFKARAANPALWRGTVSRKE
GNKCEIITKTDSQTGNKVICIFSETDQNVSIGGSGIDLINGGNVSDNVSVKAWIPAFIKM
N

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	1.7e-121	0.9972222222222222
GH13	1092	1386	1.5e-79	0.990625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09505	malS	3.39e-163	134	625	185	663	alpha-amylase; Reviewed
cd11339	AmyAc_bac_CMD_like_2	6.35e-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.
cd11338	AmyAc_CMD	7.11e-48	1067	1386	4	343	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.
cd11316	AmyAc_bac2_AmyA	7.65e-47	1068	1434	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	4.47e-46	1067	1381	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	1.71e-155	118	935	27	836
QKH59997.1	1.19e-154	134	809	44	709
BAF93484.1	1.73e-154	118	935	27	836
BAG70894.1	2.41e-154	118	935	27	836
BAB04132.1	2.41e-154	118	935	27	836

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1J0H_A	5.74e-28	1061	1471	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	1.35e-27	1061	1471	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]
5A2A_A	2.61e-27	135	564	5	327	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
2WC7_A	3.97e-27	1096	1386	51	361	Crystalstructure of Nostoc Punctiforme Debranching Enzyme(NPDE)(Acarbose soaked) [Nostoc punctiforme],2WCS_A Crystal Structure of Debranching enzyme from Nostoc punctiforme (NPDE) [Nostoc punctiforme],2WKG_A Chain A, Alpha Amylase, Catalytic Region [Nostoc punctiforme PCC 73102]
5A2B_A	4.39e-27	135	564	39	361	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P25718	1.43e-113	134	620	184	651	Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P38940	1.78e-27	1061	1471	130	544	Neopullulanase OS=Geobacillus stearothermophilus OX=1422 GN=nplT PE=1 SV=1
P14899	7.68e-27	1062	1386	32	353	Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2
Q08341	5.54e-26	1063	1386	132	461	Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
P21543	5.57e-26	136	683	744	1184	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 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
0.192925	0.790427	0.008802	0.006166	0.001119	0.000527

TMHMM  Annotations     

start	end
12	29