CAZyme Information: MGYG000000345_00192

Basic Information

• Species: UBA1829 sp002338895
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1829; UBA1829 sp002338895
• CAZyme ID: MGYG000000345_00192
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1427		160112.68	6.0068

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000345	3773289	MAG	Sweden	Europe

• Gene Location: Start: 231875; End: 236158 Strand: -

Full Sequence      

MNPVQTPAPGVHRLLYTGDVLQISLKAEGKGRAFLRTNLGNAAVRRAETVSLVDQGLASP
GQDWHDIPMMETGNGEFSIRLALIETGHFEAKAFFLPENSTAEQWPDGPNLHVNVSPAPY
CCANSIYCAFVRQFGENKTKAATGPDQMPARTAAEQELDHDHYTVIPSSGTFRALIRELD
HIFDRLKCRILHLLPINPTPTVYGRMGRFGSPYASLDFTAVNPELAEFDKKATPLEQFIE
LVDAVHSKNGKLFIDIAINHTGWASKIHEIHPEWLKRKDDGTIVSPGAWGTVWEDLTELD
YSKQELWKYIADVFITWCSRGVDGFRCDAGYMIPIPAWEYIIARVRENYPDIIFLLEGLG
GDPAVTTRLLDYANMNWAYSELFQNYSKEQVEGYLNYAWRESLGNGLMVHYAETHDNSRL
AAVSETYAKMRTALSALASMNGAFGFANGVEWFAKEKIDVHEARGLSWGATPNQVEMIGK
LNTLLLTHPAFHNGATATMIDSGSPNAVVFRRIDASGKKIVLCAVNLDCARSTVINWDPH
ASCSSGLTSYDLLSAETVDIQVVDHMRFQLELAPGEARCLSCDPDDLARIQKANASIFDR
FSKTEVQEAQSMALKCIAFLRRSLVLQKEDDPFRDAEKLLDSPEEYLKTLQPDLKDHPYI
LWKWPEDRNRNVMIPPGKFLLLVAPVRFRATLCVENEPQQEYNSLVDAKGRHFAIYYPQS
QELPHKRALLHFSAFSEGKVIRDEGHLLLLAPDILKTTVTYSHDYIRKHAPLTCMQANGR
GALMHLRLDQPAVASRYDAVMLANLSPDHPEDRHIMFRRLRIWLLHHARTQEVSLACLRN
FERAADGGAVWNYHVPTGNGLYVDISVKIEILPGKNQTRISFLRREMRGHDYLKEDASVK
LIVRPDLEDRNFHCATKASGLESVWPGKVLFKERGFEFTPAPGRTLSLTVSSGRFTPEAE
WSYMIWQPNEADRGLDPYSDTYSPGYFDFDLIDGSAVQIAASIQTADEPEKLQPARPVPA
DFHPETDLGIEYSMLNAMRAFVVKRGSLKTVIAGYPWFLDWGRDTLIAARGLVAAREFRE
DVKAILLQFARFAEHGTIPNIIHGDSVGNRDTSDAQLWLFTAAEDLCKAEHSTAFLSTEV
KDGKNLLDILEDIACDLIDGTPNGIRMDAESGLIFSPAHFTWMDTNYPAGTPREGYPIEI
QALWFAALRFLSTVSATPDRWKNLAEKVRNSIGTLFRSEDGTFLSDCLHCASGVPASQAV
KDDHIRPNQLFAITLGAVDDKEFGRSILDATSCLLVPGAIRSLADRPTRYPLPIRGADGQ
LLNDPNRPFWGSYEGDEDTRRKPAYHNGTAWSWPFPSYCEAYAMMYEKTGAAVARSLLSS
CEMIMRTGCVGQIPEILDGNYPHRQRGCDAQAWGMTEYYRVWKLLHQ

Enzyme Prediction     

No EC number prediction in MGYG000000345_00192.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH133	1047	1419	4.8e-91	0.9731182795698925
GH13	186	370	9.1e-31	0.8428571428571429
GH13	304	437	5.7e-18	0.36533333333333334

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06202	GDE_C	2.89e-76	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	1.77e-53	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	9.97e-38	953	1420	178	601	Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	1.63e-26	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.
cd11344	AmyAc_GlgE_like	4.79e-25	167	489	17	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABC78593.1	0.0	1	1425	1	1420
AQV01271.1	0.0	4	1422	8	1429
AOY59008.1	0.0	4	1422	8	1429
BBO75755.1	0.0	4	1422	8	1425
ABW66661.1	0.0	5	1425	16	1431

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	1.57e-33	169	457	26	319	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	9.20e-18	178	526	26	365	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]
1CYG_A	1.93e-11	213	526	96	431	CyclodextrinGlucanotransferase (E.C.2.4.1.19) (Cgtase) [Geobacillus stearothermophilus]
1CGY_A	2.55e-11	213	496	89	409	ChainA, CYCLOMALTODEXTRIN GLUCANOTRANSFERASE [Niallia circulans]
7EKW_A	3.57e-11	1034	1362	1042	1441	ChainA, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138],7EKW_B Chain B, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9JN46	1.64e-25	170	528	212	585	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Fragment) OS=Cereibacter sphaeroides OX=1063 GN=glgE PE=3 SV=2
Q3J3M8	1.85e-25	170	528	230	603	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
Q2RTZ1	2.28e-23	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	1.18e-17	170	542	676	1057	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Burkholderia pseudomallei (strain K96243) OX=272560 GN=glgE PE=3 SV=2
Q9I1W4	3.78e-17	170	528	227	601	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
1.000045	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000345_00192.