CAZyme Information: MGYG000000538_01579

Basic Information

• Species: UBA1829 sp900549045
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1829; UBA1829 sp900549045
• CAZyme ID: MGYG000000538_01579
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1427		159120.81	6.7116

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000538	3384359	MAG	Fiji	Oceania

• Gene Location: Start: 102932; End: 107215 Strand: +

Full Sequence      

MTPIQTPAPGSHRLLYTGDVFQVTLKTAGAGRAFLRTNLGNAAVRRAETISVVDRGLASP
GQDWHDIPMTDLGNGEFTIRLALVETGHFEAKAYFIPADSTTELWPDGQNVHVNVSPAPY
CCANSIYCAFIRQFGENKTLASTDRSIRPFRAMAENELDHENYTVIPSSGTFRALIRELD
HIFDRMKCRILHLLPVNPTPTVYGRMGRFGSPYASLDFTAVNPELAEFDKTATPLEQFLE
LVDAVHSKNGKLFIDIAVNHTGWASKIHEIHPEWLKRRDDGTIVSPGAWGTVWEDLTELD
YSKKDLWKYIADVFIIWCRRGVDGFRCDAGYMIPVPAWEYIIARVREQFPDIIFLLEGLG
GDPAVTTRLLDYANMNWAYSELFQNYSKEQIEGYLNYAWRESNGNGLMVHYAETHDNSRL
AAVSENYARMRTALSALASVNGAFGFANGVEWFAKEKIDVHESCGLSWGATPNLVEFIGK
LNTLLLTVPAFHNGASMTFLNSGSPNAVVFRRTGASGNGTVLCAVNLDCEHPALIQWNAD
DAGACGLAAYDLISARAVAVKPVGTMRFQLKLAPGEALCLSGEPRDLLRIREASAKIFDR
FSKSEVQEAQAMALKCIAFLRRSVVLQPDDDQNAAAKALLESPEAYLKTLQPDLKDHPYV
PWRWPEDAHRKVMVPPGKFILAVAPFRFRASLNIENGNPQEHNSLVDARGRHFAIFYPQT
QELPHKRAVIRFSAFSGGKVQRSEGHLLLLAPDILATALSYSHDYIRKYAPLSCIQANGR
GALMHLRLDQPDVSSRYDAVMLANLSPDHPEDRHIMFRRLRVWVLHHARTQEVSLVCLRN
FERAADGSCIWNYHVPTGNGLYTDISLKIEMVAGKNQTRVSFLRRDTHGHEYLEPENPVK
LIVRPDVEDRNFHYSTKANGLESVWPGKVNFRERGFDFTPAPGRTLTLTASSGRFVPAAE
WNYMLWQPNEAARGLDPYSDVYSPGYFEINLTGGGSVQIAASILTGAEPDALSPVKVTSA
DFRAATDSGIETNMLDAMRAFVVKRGDLKTVIAGYPWFLDWGRDTLIAARGLIAAREFRN
DVKAIIRQFAMFAEQGTIPNIIHGDTVGNRDTSDAQLWLFTAVEDLCKAERSNDFLKTEV
RPGKTILDKLEEIAACLIAGTPNGIKTDPASGLVFSPPHFTWMDTNYPAGTPREGYPVEI
QALWFAALRFLSTVSATPERWKTLAEKVRASIRTLFLSDDGKYLSDCLHCSAGTPAAKAV
KDDHIRPNQIFAITLGAIDDKELGRSILDTAACLLIPGAIRSLADKPTRYPLPVRDTNGN
LLNDPSHPYWGRYEGDEDTRRKLAYHNGTAWTWPFPSYCEAYAMMYEKTGAAVARSLLSS
CEMIMRNGCVGQLAEILDGDYPHTQRGCDAQAWGMTEYYRVWKLLHR

Enzyme Prediction     

No EC number prediction in MGYG000000538_01579.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH133	1047	1419	1.2e-92	0.9731182795698925
GH13	178	370	3.4e-30	0.8761904761904762
GH13	303	437	1e-18	0.368

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06202	GDE_C	4.17e-80	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	7.23e-55	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	7.79e-37	884	1420	123	601	Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism].
cd00551	AmyAc_family	2.93e-27	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.
pfam12439	GDE_N	6.59e-27	794	997	22	208	Glycogen debranching enzyme N terminal. This domain family is found in bacteria and archaea, and is typically between 218 and 229 amino acids in length. The family is found in association with pfam06202. Glycogen debranching enzyme catalyzes the debranching of amylopectin in glycogen. This is done by transferring three glucose subunits of glycogen from one parallel chain to another. This has the effect of enabling the glucose residues to become more accessible for glycolysis.

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
AQV01271.1	0.0	4	1422	8	1429

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3DHU_A	4.11e-32	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	526	24	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]
1WZA_A	3.80e-10	170	350	24	227	Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii]
5CGM_A	5.20e-10	167	357	248	444	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	1.17e-09	213	536	100	445	ChainA, CYCLOMALTODEXTRIN GLUCANOTRANSFERASE [Niallia circulans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9JN46	1.58e-24	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	1.73e-24	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	1.53e-19	170	542	676	1064	Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Burkholderia pseudomallei (strain K96243) OX=272560 GN=glgE PE=3 SV=2
Q9I1W4	2.87e-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
1.000073	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000538_01579.