CAZyme Information: MGYG000000360_01246

Basic Information

• Species: UBA1829 sp900548385
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1829; UBA1829 sp900548385
• CAZyme ID: MGYG000000360_01246
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1427		159435.82	6.1314

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000360	4492877	MAG	Sweden	Europe

• Gene Location: Start: 570758; End: 575041 Strand: -

Full Sequence      

MTPIQTPAPGSHKLLYTGDVFRITLSVSGKGRAYLRTNLGNAAVRRAETISLVDRGLVSP
GQDWHDIPMADLGNGEHAIRLALVETGHFEAKAFFIPENSTVEQWPDGPNIHVNVSPAPY
CCANSIYCAFIRQFGENKTLASTDGALRPERTAAENELDRSGYSVIPSSGTFRGLIRELD
HIFDRMKCRILHLLPINPTPTVYGRMGRFGSPYASLDFTAVNPELAEFDRKATPLEQFIE
LVDAVHSKNGKLFIDIAVNHTGWASKIHETHPEWLKRRPDGTIVSPGAWGTVWEDLTELD
YNNKELWKYIADVFVIWCERGVDGFRCDAGYMIPVPAWEYIIARVREKYPDIIFLLEGLG
GDPAVTTRLLDYANMNWAYSELFQNYSKEQIEGYLNYAWKESLGNGLMVHYAETHDNARL
AAVSQNYARMRTALSALASMNGAFGFANGVEWFAKEKIDVHEARGLSWGAEPNLVDYIGK
LNTLLLTHPAFHNGATAAFIDSGTPDAVLFRRIDASGKKVVLCAVNLNCEHATVVRWNPH
ESYSCGLAAYDLLSAETVNVKAVEHMLFRLELAPGEARCLSCDSDDLVRIQEASAKIFDR
FSKSEVQEAQSMTLKCTAFLRRSVVLQPEDDPYRAAGALLESPEQYLKTLQPDLKDHPYV
IWKWPEDTRRNVMITPGKFILLLAPVRFRATLCVENEYSQEHNSLVDAQGRHFAIYYPHA
QELPHKNAILKFSAFSDGKVIRDEGHLLLLAPDILNTALRYSHDYIRNSAPLTCMQANGR
GALMHLRLDQPAVSSRYDAVMLANLSPELPEDRHIMLRRLRIWLLHHARTQEITLACLHD
FERAADGAAIWNYHVPTGNGLYVDISMKIEIVAGKNQTRITFLRKEGSGRDYLASGSAVK
LIVRPDVEDRNFHYSTKASGLENVWPGKVRFLERGFDFTPAPERTLSLQTSSGKFVPGAE
WSYMIWQPNEADRGLDPHSDTYSPGYFDIDLDDCGSAQISASIQTPMEPEKLQPVKPSAA
DFRAAEDSGIETNMLAAMRAFVVKRGELKTVIAGYPWFLDWGRDTLIAARGLIAAPEFRG
DVKAILRQFAQFAEHGTIPNIIHGSTVGNRDTSDAQLWLFTATEDLCKAEQSTEFLRTEI
KDGKTLLDKLEEIAADIIAGTPNGIKTDPESGLVFSPPHFTWMDTNYPAGTPREGYPVEI
QALWFAALRFLSGVSGTPDRWAALAEQVRTSIRTLFLSDDATCLSDCLHCSSGTPARLAV
KDDHIRPNQLFAITLGAIDDKELGRSILDAASCLLVPGAIRSLADRPTRYPLAIHGNNGE
LLNDPLHPYQGTYEGDEDTRRKPAYHNGTAWSWPFPSYCEAYAMMYEKTGAAVARSLLSS
CEMVMRTGCVGQIAEILDGNYPHRQRGCDAQAWSMTEYYRVWKLLHR

Enzyme Prediction     

No EC number prediction in MGYG000000360_01246.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH133	1047	1419	2.3e-91	0.9731182795698925
GH13	178	370	1e-32	0.8761904761904762
GH13	303	437	1.6e-18	0.368

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06202	GDE_C	5.16e-79	1040	1420	5	374	Amylo-alpha-1,6-glucosidase. This family includes human glycogen branching enzyme AGL. This enzyme contains a number of distinct catalytic activities. It has been shown for the yeast homolog GDB1 that mutations in this region disrupt the enzymes Amylo-alpha-1,6-glucosidase (EC:3.2.1.33).
cd11313	AmyAc_arch_bac_AmyA	2.00e-57	126	494	7	336	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.
COG3408	GDB1	2.14e-40	883	1420	108	601	Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
cd11344	AmyAc_GlgE_like	1.17e-31	160	489	10	355	Alpha amylase catalytic domain found in GlgE-like proteins. GlgE is a (1,4)-a-D-glucan:phosphate a-D-maltosyltransferase, involved in a-glucan biosynthesis in bacteria. It is also an anti-tuberculosis drug target. GlgE isoform I from Streptomyces coelicolor has the same catalytic and very similar kinetic properties to GlgE from Mycobacterium tuberculosis. GlgE from Streptomyces coelicolor forms a homodimer with each subunit comprising five domains (A, B, C, N, and S) and 2 inserts. Domain A is a catalytic alpha-amylase-type domain that along with domain N, which has a beta-sandwich fold and forms the core of the dimer interface, binds cyclodextrins. Domain A, B, and the 2 inserts define a well conserved donor pocket that binds maltose. Cyclodextrins competitively inhibit the binding of maltooligosaccharides to the S. coelicolor enzyme, indicating that the hydrophobic patch overlaps with the acceptor binding site. This is not the case in M. tuberculosis GlgE because cyclodextrins do not inhibit this enzyme, despite acceptor length specificity being conserved. Domain C is hypothesized to help stabilize domain A and could be involved in substrate binding. Domain S is a helix bundle that is inserted within the N domain and it plays a role in the dimer interface and interacts directly with domain B. 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	4.60e-28	170	442	22	247	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
ABC78593.1	0.0	5	1425	7	1420
BBO84810.1	0.0	5	1422	9	1424
BBO91312.1	0.0	5	1422	9	1424
ABW66661.1	0.0	5	1425	16	1431
BBO75755.1	0.0	4	1422	8	1425

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	9.89e-36	146	484	2	346	Crystalstructure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_B Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_C Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_D Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum]
4GKL_A	6.76e-20	172	534	24	373	Crystalstructure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana],4GKL_B Crystal structure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana]
5CGM_A	4.78e-14	167	578	248	691	Structureof Mycobacterium thermoresistibile GlgE in complex with maltose at 1.95A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CGM_B Structure of Mycobacterium thermoresistibile GlgE in complex with maltose at 1.95A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CIM_A Structure of Mycobacterium thermoresistibile GlgE in complex with maltose (cocrystallisation with maltose-1-phosphate) at 3.32A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CIM_B Structure of Mycobacterium thermoresistibile GlgE in complex with maltose (cocrystallisation with maltose-1-phosphate) at 3.32A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CJ5_A Structure of Mycobacterium thermoresistibile GlgE APO form at 3.13A resolution [Mycolicibacterium thermoresistibile ATCC 19527],5CJ5_B Structure of Mycobacterium thermoresistibile GlgE APO form at 3.13A resolution [Mycolicibacterium thermoresistibile ATCC 19527]
1CGY_A	4.21e-13	213	560	89	471	ChainA, CYCLOMALTODEXTRIN GLUCANOTRANSFERASE [Niallia circulans]
1WZA_A	4.81e-13	170	350	24	227	Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q2RTZ1	1.84e-28	170	528	255	628	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1) OX=269796 GN=glgE PE=3 SV=1
Q63T93	2.29e-20	160	531	666	1053	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Burkholderia pseudomallei (strain K96243) OX=272560 GN=glgE PE=3 SV=2
Q6L2Z8	1.04e-19	161	528	190	569	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828) OX=263820 GN=glgE PE=3 SV=1
Q1D651	3.47e-19	210	528	269	594	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Myxococcus xanthus (strain DK1622) OX=246197 GN=glgE PE=3 SV=1
Q9I1W4	7.94e-19	161	542	210	605	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=glgE PE=3 SV=1

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
1.000044	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000360_01246.