CAZyme Information: MGYG000003528_02554

Basic Information

• Species: CAAGGB01 sp900769285
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; UBA1407; UBA1407; CAAGGB01; CAAGGB01 sp900769285
• CAZyme ID: MGYG000003528_02554
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1423	MGYG000003528_319|CGC1	154478.64	5.6204

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003528	3662993	MAG	Fiji	Oceania

• Gene Location: Start: 5863; End: 10134 Strand: +

Full Sequence      

MSSVELSLEQEPAAGSEVLAYSGDVLTFELYVGGEAEGTGYVRTSLGGSAALLDEAIREV
DGGASPSGAAWRDVAMRPVGDGRFRCTLPLCEVGVFEAKCLFVTAADGGCHWVPGANVRI
KVEPAGTTARNAIYNAFVRQFGRYAAGPGRGEDSLRAEGFLDGQEYTVLPPSGRFRDVLR
QLPHIMGTLGFRILQLLPVQPPPTTYARMGRYGSPFAPVDYFCVDPSMAEFDHRTTPLEQ
FGELVDGVHARGGLVLLDLPIDHTGWASSLQVEHPEWFCRNGDGSFASPGAWGVVWEDLC
KLDFSHRGLWRYLAEVFLHWTRHGVDGFRCDAGYMVPCEVWRYIVARVRRQYPDTLFFLE
GLGGPTETTARLLSSGGMDWAYSEIFQVYGREPLAGYLAHLLRGGAGLGVAVNFAETHDN
ARLASVSPAWAAMRTALAALTSQTGAFGVANGVEWLATEKIDVHGASSLNWGAEPNLVAH
LRRLNDILAALPAFGAAARCRLVGDGTALGVLRTTGVAAETVLAVLNPEEHSPAWLEWQE
GEFGGQDLHDLLADSHVSAARLPGGRWRLELAPAAAVCLSPRPLDSWLAERRDENGDQRR
RQAVLRAWVAVRGLADVPDDQPERWCRQLADSPEAFLRELTGEAIAPLTVWEPSRDGRRV
VPLPAHHFLLVRESCPFRVSLHDGETRLDGAESFASSDGGWLAPLPPAPSAPVAAWRLEL
RLERYVSAAEVRRVSGQVLRLPEPGRCQVRLSLPAAELTARHLGLCSNRRGSYTQARARW
GELHSKYDALLAASLEEGHPADRFAALLRCRAWLVHRGASAELDPACQTGFAAGYDNTLV
WTFAAPAGLGGRIGLTVTLRLSPERNAGTLTFSRSADDADAADGREPVELIMRPDVDWRV
NHGVTAAYTGPEHDFPNGVTAWARGFAFRPSGAAAGLEMEADAGAFAKDGAWTYQVGLDE
DAQRCLPDRTDVFSPGYFRWQLHADARVTCRFAIAGEPLSDMAAPDGAAALPSRLPLGEA
LRRSLERYLADRDGGRTVIAGFPWFLDWGRDTLICLRGLVAAGRLDDCRGIIRAFASFEE
QGTIPNMIRGADSGDRATSDAPLWLLAAAEALHDALPAGERAALLQLDCGGRPLLAILES
LAWHYRSRLPNGICCDSASGLVFSPPHFTWMDTNYPAGTPREGYPVEIQSLWLHALAFLS
RVTGKGCYADWRALAADSFRRLYVRADGLGLHDCLLGPSGRPAADCTPDDAIRPNQLLAL
TLCPDCVPPSARRAALSVCAGLLVPGSIRSLDDRPLSVPLPIVRDGVPLNDPHHPYWGQY
GGDEDTRRKAAYHNGTAWGWQMPLYCEALARECPFDDGALRTARALLETAALAMEAGCLG
QMAEIYDGDAPHAGRGCPAQAWSMSEAYRVWRLLEARRLEAGR

Enzyme Prediction     

No EC number prediction in MGYG000003528_02554.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH133	1034	1408	1.2e-81	0.9731182795698925
GH13	180	383	1.6e-31	0.9238095238095239

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06202	GDE_C	6.00e-64	1034	1409	17	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	7.42e-52	128	487	1	326	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	1.94e-36	950	1409	184	601	Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	3.74e-27	133	445	2	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.
cd11344	AmyAc_GlgE_like	2.89e-25	172	487	19	350	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBO75755.1	0.0	7	1411	6	1425
BBO70997.1	0.0	7	1411	6	1425
AKJ63770.1	0.0	8	1410	11	1419
BBO84810.1	0.0	7	1411	6	1424
QSH41975.1	0.0	22	1414	14	1414

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	7.41e-32	172	457	26	316	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]
5CGM_A	2.76e-14	170	540	248	641	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]
1WZA_A	1.50e-06	183	331	41	197	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
Q3J3M8	3.49e-19	166	573	215	651	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) OX=272943 GN=glgE PE=3 SV=3
Q9JN46	6.38e-19	166	454	197	499	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Fragment) OS=Cereibacter sphaeroides OX=1063 GN=glgE PE=3 SV=2
Q8KAR6	3.45e-16	173	401	228	461	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) OX=194439 GN=glgE PE=3 SV=1
B3DYJ8	3.09e-15	173	554	227	633	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Methylacidiphilum infernorum (isolate V4) OX=481448 GN=glgE PE=3 SV=1
Q8PE50	9.22e-15	162	365	215	420	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 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
1.000018	0.000015	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003528_02554.