CAZyme Information: MGYG000000596_01205

Basic Information

• Species: UBA1724 sp900548225
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; UBA1407; UBA1407; UBA1724; UBA1724 sp900548225
• CAZyme ID: MGYG000000596_01205
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1429	MGYG000000596_12|CGC2	159294.32	6.6095

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000596	2231726	MAG	Madagascar	Africa

• Gene Location: Start: 56534; End: 60823 Strand: -

Full Sequence      

MDPVQVILEQHPAPHAHIVRHAGDTIRITLKLSRPIRGRAFVRTNLGNASIQRTETIDKV
EMGIEPLGRDWQDIPMRQVDATTFAAHLALVEIGVFDFKCFFYNETTGKALWPRGENGRV
KVISAEGVARNTIYNAFVRQFGENISGKAASPELASAAEFLDKRNFTVIPPSGTFRAIQS
KLDFILGDLGFRILQFLPVHPIPTTFARMGRYGSPFAPLDFMDVDASMAEFDQRTTPLEQ
FLQLVDQVHARGALVFLDIPIDHTGWASVLQSHHPEWFARTADGAFQSPGAWGVVWADLC
KLDFTKTDLWKRMAEVFIHWCRNGVDGFRCDAGYMVPAPVWKYIVAKVRQQFPDTIFFLE
GLGGGQDATTRLLDDSDLDWAYSELFQNYTQQELSRYLDFATGYSAAHGALVNFAETHDN
DRLAAKSKEWARLRVALSALFAPAGCFGIANGVEWYATEKIDVHGARSINWGSADNMVPL
LSSLNALLGSHPAFRADARLRIPYGASGDAVGILREPRKDVEHALLVVANPRPDACAAYH
WHYQEFEAGSRPTDILTGKQLSASLGECLYTINLEPGQVVCLCKPGKQKLAEQPYGARER
QLLRATALRLRCSLWGYGDLDGAEPEDDAYALFQDPHSFIQKVSGEKHYLPLVEWSPEKD
GQRVAILPDDHYLLICDRRPFRAQLLFDGTVRQRCESMPRKDGQNFAVLLPPVRRITRTT
TALIQVTCYDEGAKVVKYEAEILLLPLNAPLSVMRRVTRHELTRRHSFLAANSYGSYALI
RGMWGNLEGQYDALLAANQNPELPADRTVVFPRLRAWLVHHDYSQEINVNCQTDFVVTGP
NSASWHFIIPSGIGGNAYISISYVLDKERNAFTISFTRCPPPEESDAFPAMDEHSPVTLI
LRPDIDDCCNHNPTQAYLGAENAFPQRLKTGNDGFSFTLESKNRLEARISRGVFVGDSEW
TYNFHDALEEERGLRATRDLYSPGHFRLDLRRGETAVLSAALLTPSEPPMDAPVEPDAPI
PFHENNAKVPLKTALEEALGAFIVRRNPLKTIIAGYPWFLDWGRDTLICLRGLIAAGRLD
DALAIIVQFASYERKGCLPNMISGEQVSNWDTSDAPLWLFNAVSEYMRAVGKNLSQKVLA
TPCGKRSLLQVLESIAASYMKGTENGIAMDAASGLVFSPSHFTWMDTNYPAGTPREGYPI
EIQAFWYGALDLLAKHTGKSIYVTTAKRVKESVAKYYVSRPDVGLSDCLHGRPGTPAAKA
TADDACRPNQLFALTVPGLIDDFELQQTVIAATGHLLVPGGMRTLANQRVEFLQPIYKDG
HLLNNPAFPYWGEYIGDEDTRRKPAYHNGTAWAWLMPSFCEALLRTFGPSAKPAARSLLH
TTAALMRRGCVGQLPEILDGDIPHKTRGCCAQAWSVTEAYRILRMMERE

Enzyme Prediction     

No EC number prediction in MGYG000000596_01205.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH133	1048	1420	1.1e-93	0.9731182795698925
GH13	188	372	1.9e-31	0.8428571428571429
GH13	307	438	3.5e-18	0.36

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06202	GDE_C	1.76e-79	1041	1421	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	1.99e-52	164	495	13	334	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	7.08e-41	939	1423	164	603	Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	4.12e-26	164	445	8	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	5.48e-24	172	492	19	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
AKJ63770.1	0.0	8	1423	11	1420
QSH41975.1	0.0	22	1429	14	1417
BBO75755.1	0.0	10	1422	9	1424
ABC78593.1	0.0	4	1427	1	1421
BBO70997.1	0.0	8	1422	7	1424

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	2.44e-31	172	511	26	378	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]
1JF6_A	1.91e-07	173	580	170	581	ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF6_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1WZL_A	2.51e-07	173	580	170	581	ChainA, Alpha-amylase II [Thermoactinomyces vulgaris],1WZL_B Chain B, Alpha-amylase II [Thermoactinomyces vulgaris]
1WZM_A	2.51e-07	173	580	170	581	ChainA, Alpha-amylase II [Thermoactinomyces vulgaris],1WZM_B Chain B, Alpha-amylase II [Thermoactinomyces vulgaris]
1BVZ_A	2.51e-07	173	580	170	581	Alpha-amylaseIi (tvaii) From Thermoactinomyces Vulgaris R-47 [Thermoactinomyces vulgaris],1BVZ_B Alpha-amylase Ii (tvaii) From Thermoactinomyces Vulgaris R-47 [Thermoactinomyces vulgaris],1JI2_A Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2 [Thermoactinomyces vulgaris],1JI2_B Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2 [Thermoactinomyces vulgaris],3A6O_A Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/acarbose complex [Thermoactinomyces vulgaris],3A6O_B Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/acarbose complex [Thermoactinomyces vulgaris]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q3J3M8	6.42e-27	173	549	230	620	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	1.27e-26	173	541	212	594	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Fragment) OS=Cereibacter sphaeroides OX=1063 GN=glgE PE=3 SV=2
Q63T93	1.18e-17	173	544	676	1055	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Burkholderia pseudomallei (strain K96243) OX=272560 GN=glgE PE=3 SV=2
B3DYJ8	5.97e-16	153	571	207	637	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Methylacidiphilum infernorum (isolate V4) OX=481448 GN=glgE PE=3 SV=1
Q1D651	2.35e-15	174	554	222	616	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Myxococcus xanthus (strain DK1622) OX=246197 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
1.000031	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000596_01205.