CAZyme Information: MGYG000000467_01688

Basic Information

• Species: CAAGED01 sp900768505
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; CAAGED01; CAAGED01 sp900768505
• CAZyme ID: MGYG000000467_01688
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1430		161991.82	5.8777

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000467	2445290	MAG	Fiji	Oceania

• Gene Location: Start: 17273; End: 21565 Strand: +

Full Sequence      

MKQFIFPERRIFNRGDLLTFRLECPNAEVGDAAFVRTNLGMAGVRRREIINHVEHELPIL
GSDWHDIPMKRLSPGIYQLVLPLLEVGVFEAKCFLMNHISEREAWPQGGNFRLKIEPSEN
ISGNTIYTAFVRQFIRKPHPAADSIANLTELEKAGYTIIPPSGTFRGLIEKLDFIFGTLR
SRILQLLPIHPAPATYARMGRYGSPFAALDYFDVDPALAEFDPTASPMEQFDELIEQVHA
RNGRIFMDIPVNHTGWASKLQEAHPEWFVRDAAGKFISPGAWGVTWGDLCKLDYTQEEVC
NFMAEVFLFWCRRGVDGFRCDAGYMLPVAAWDYINAKVREEFPDTVFMLEGLGGPWDKQS
QLLEQSGLNWAYSELFQNYSRSQIESYFPVMYNVSRNSGLLVNFAETHDNNRLAAVSVKF
AQMRTALCALLSLNGAFGFANGVEWFANEKIDVHSCNDLNWGSKNNQVDFIRRLQILLEA
HPAFGNSGEIQLITRSGVECLAVLRQSRQFDGGAISPLLILVNLDCQQSQSVEFDGRGIN
WSNAADLLTGEPFEILEQPNKLCKLLLSPGQTLVLISTADPLYGEIRDKINYPLHICPGE
NRQIILQRARAMMFRAITLLKNDLDLSDLDNPDADCMKFLNSPLQYCRNIIASPISRVMV
IDPVRDCRRNVMLPQRGLLLVRHHAKFRMVLKYGDMTLRSGMSVPGAHEHFTLLCIPHNR
IKRNVKLTMYLSAYTPSGKTSNFTVHMQLLPDCEDNEIRTIFQRERVIDENIYAFGSNER
GSYTMFPAAFGSLRSKYDALLSANGQTPYPTERTTMLTRCRMWLVCYGYSQQLDVEKLLN
YTGSVDNRGSWLFRVPVGQGKSVTLKMQFKFSETSDAVTLLFHRYACRSEDELPDRVPVK
LIIRPDVESRINHQLTKAFTGPEKLFPASVIAGRDTFEFSPYDHKLIVSLADGEFHPEPQ
WNYMVELPLEKYYGLECNTDLFSPGYFQYKLKGDQICLLRCVVNEDLAQAPTLEDFKDPL
PDRLQLSDALPRALRRYVVRRDDHKSIIAGYPWFLDWGRDTLIALRGIIAAGMQNEAQDI
LLQFAKYEENGTLPNMIRGNDVSNRDTSDAPLWFFVAAGDYMEQNGDEILQADCGNGRTL
LEVMNSIFTNYVKGTPNGIRMDESSKLVYSPAHFTWMDTNYPAASPRAGYPVEIQALWYN
AVRVLKDYNSHAAQILPEIRHSIIQYFYHPESSSFSDCLLANEFTAAADALPDDAVRPNQ
LFLLTLGVLDEKLHCGSILQSATDLIVPGAIRSLSDRRLDVPLPVNWLGQLLNDPYHPYR
GIYSGPEDTSRKVAYHNGTCWMWPFPSYCEAIYIIGGESARSLALSILLSAKYYLECGAV
GQLPEVADGDYPHTSGGCPAQAWSMTEFYRVYRKLQKSPSTDETMEKTNS

Enzyme Prediction     

No EC number prediction in MGYG000000467_01688.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH133	1042	1409	2.6e-86	0.9758064516129032
GH13	162	445	1e-28	0.919732441471572

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06202	GDE_C	7.61e-75	1037	1410	6	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	3.40e-47	125	486	6	335	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	2.48e-39	953	1404	178	595	Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	4.45e-32	125	435	1	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.
cd11349	AmyAc_3	8.49e-22	200	414	80	356	Alpha amylase catalytic domain found in an uncharacterized protein 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; 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
QSH41975.1	0.0	1	1415	1	1414
AVM43688.1	0.0	1	1416	1	1403
ABC78593.1	0.0	15	1418	20	1423
QBG47427.1	0.0	8	1416	12	1400
AKJ63770.1	0.0	14	1415	25	1423

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	7.75e-26	162	450	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]
1WZA_A	1.36e-11	163	332	24	209	Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]
5OT1_A	1.63e-09	163	413	349	605	ChainA, Pullulanase type II, GH13 family [Thermococcus kodakarensis]
5BRQ_A	9.16e-09	163	321	37	209	Crystalstructure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_B Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_C Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_D Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580]
1UOK_A	1.19e-08	163	321	28	199	CrystalStructure Of B. Cereus Oligo-1,6-Glucosidase [Bacillus cereus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q6L2Z8	1.26e-18	156	531	192	575	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
Q3J3M8	4.55e-16	163	535	230	613	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	8.80e-16	163	534	212	594	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase (Fragment) OS=Cereibacter sphaeroides OX=1063 GN=glgE PE=3 SV=2
Q2RTZ1	3.22e-15	163	557	255	656	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
Q8KAR6	6.41e-14	163	554	228	644	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

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
1.000054	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000467_01688.