CAZyme Information: MGYG000001795_01694

Basic Information

• Species: Amulumruptor caecigallinarius
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Amulumruptor; Amulumruptor caecigallinarius
• CAZyme ID: MGYG000001795_01694
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1083	MGYG000001795_10|CGC2	119571.32	4.3954

Genome Property

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

• Gene Location: Start: 70030; End: 73281 Strand: -

Full Sequence      

MKHLKKMLCGSLIAFGTLAQQASAATFVGDRTDFRDETIYFAMTTRFYDGDPNNNVYCWD
GVLNVNDPEWRGDFAGLIKKLDYIKALGFTAVWITPIVENGSGLDYHGYHAMDFSKIDHR
YVSKESTDADADVAFQTLIDEVHKRDMKLILDIVLQHTGNFGEAKLCRMFQKDYTQDLGD
INASMIVVPQSEGGQLPEDYPAMKPGDQYATRLAMMKNSDFTNRDIHNYWHHKAWFDWDD
PSRWWGQIAGDCVDLNTEHPAVAEYLVECYSRFIKMGVDGFRIDTAGHIPRLSFNNNFLP
QLMEAANSAEAKAKRGDTPFFMYGEVCARSMEVIYRGENYNCSPCYYTWKESKNYPWDYD
PTSWDSVVAIPTPTEGSHDYFTVQGHTNWESVLQSGIDDLGHADAILRKSDNALLNGNEY
HTPDYSDYSGMSVIDFAMHWNFKSASGAFGVHGQDNLYNDATYNVVYVDSHDYAPDSNYR
FEGTQDTWAENLSLMFTFRGIPCLYYGSEVEFQKGKPIDKGAVEALKDTGRAYFGGYIEG
DLTVTDFAEYSGATGNIASTLTYPLARHIQRLNKIRAAVPALRKGQYSTDGCSGSMSFKR
RYVDDNTDSYVLVTISGSSTFTGILNGTYVDAITGDTKTVTDGTLTATCSGKGNLRVYVL
NTSKTPAPGKVGEDGKYLYGTASVDQPWTEWPDETMPEETWTVKPSGGGSGGTVEEPEEP
IEPAIEDGEQAIFFENTSDWGGYIYAWIWNDDGNYTGGNWPGQVLTYLGNKIWKWTYTGT
ETIPDDAVIIFSNGSDQVPGRDQGGFDFVNGGYYTQDGYLKTIEPETTSPRVSMSPNGGD
FIESVTVTLKANSVTTSATYKVGNASEVSFTGTTTVTIGEDMEVGESVTISWTATDGTAT
TNGKATFTKVEKPAGITIYADNSEVQWSPLKIHHFDVDASTWPGVDMLKVAENIYTYTVP
DGTRGVVFNNGQGNGSNQTEDYTNLTNNHLYLIKPNGSNKATVEDKGVYGGASIDDLYVN
DLYAGIEISLVPGGILVSASVDGMVHISTISGQTRSIAVTPGQTLIDGLEGFYIVNGQKL
FVK

Enzyme Prediction     

EC	3.2.1.59

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	71	515	1.9e-123	0.997624703087886

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11339	AmyAc_bac_CMD_like_2	7.87e-108	35	579	1	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.
cd11320	AmyAc_AmyMalt_CGTase_like	3.80e-44	33	509	1	348	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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.
cd11340	AmyAc_bac_CMD_like_3	1.17e-36	38	523	5	366	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.
pfam00128	Alpha-amylase	1.13e-35	72	510	1	326	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	7.22e-34	38	326	2	246	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNT65573.1	3.83e-250	1	949	1	1003
QNT65572.1	1.77e-242	1	981	1	1044
QNT65571.1	1.01e-240	20	981	8	1041
BCJ94880.1	3.46e-216	33	678	247	848
APB78307.1	8.75e-214	28	678	347	948

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4E2O_A	1.50e-29	34	607	7	394	Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
5A2B_A	1.58e-26	10	377	18	283	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]
5A2A_A	2.33e-26	34	377	6	249	CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
1QHO_A	2.12e-21	35	533	7	389	FIVE-DOMAINALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE/ACARBOSE COMPLEX [Geobacillus stearothermophilus],1QHP_A Five-Domain Alpha-Amylase From Bacillus Stearothermophilus, Maltose Complex [Geobacillus stearothermophilus]
6WNI_A	1.97e-20	35	290	32	256	ChainA, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNI_B Chain B, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNU_A Chain A, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P21543	6.94e-28	16	308	732	960	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
Q05884	8.23e-22	72	618	98	565	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P19531	1.81e-21	7	533	13	422	Maltogenic alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyM PE=1 SV=2
P08704	8.07e-21	33	325	39	287	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt PE=3 SV=1
P30921	2.58e-19	22	290	27	262	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 17-1) OX=72572 GN=cgt 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
0.000371	0.998795	0.000232	0.000212	0.000196	0.000187

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001795_01694.