CAZyme Information: MGYG000002713_01934

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA1381; UBA4716
• CAZyme ID: MGYG000002713_01934
• CAZy Family: GH65
• CAZyme Description: Nigerose phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
233		25673.58	7.6804

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002713	2668614	MAG	Canada	North America

• Gene Location: Start: 33; End: 734 Strand: +

Full Sequence      

MAKFVFDAALELSEKCPIESELKERLKDSSKNILIKEPNASGIIEQFDGYFKLEDASVDT
VRSRLINPKEYWGGAYGVAADTQVIKQADVVAMLSMFKNDYTSDIMAKNLKYYEPRTEHG
SSLSACMYSLLACYTNNPEIAYPMFMKSAKADLVKGGKEWAGLIYIGGTHPASAGGAWIA
AVKGFAGISEENGHLVCRPNLPEKWNGMTFKLIYKGKKYLVKIQDGNGAISII

Enzyme Prediction     

EC	2.4.1.279

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH65	1	190	6.4e-44	0.5080645161290323

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1554	ATH1	1.10e-48	1	224	508	734	Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
pfam03632	Glyco_hydro_65m	2.44e-35	1	195	190	387	Glycosyl hydrolase family 65 central catalytic domain. This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom. The catalytic domain also forms the majority of the dimerization interface.
PRK13807	PRK13807	1.72e-26	85	223	589	722	maltose phosphorylase; Provisional
pfam03633	Glyco_hydro_65C	5.33e-04	199	223	1	25	Glycosyl hydrolase family 65, C-terminal domain. This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The C-terminal domain forms a two layered jelly roll motif. This domain is situated at the base of the catalytic domain, however its function remains unknown.
COG3459	COG3459	0.001	173	233	967	1027	Cellobiose phosphorylase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCK00434.1	4.64e-79	1	223	482	710
ABX43667.1	1.52e-78	1	223	501	738
ABX42243.1	1.84e-76	1	233	504	751
QLY80561.1	3.15e-76	1	233	482	725
SET84809.1	9.11e-74	1	233	481	722

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KTP_A	1.42e-37	12	223	512	724	ChainA, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTP_B Chain B, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10]
4KTR_A	1.42e-37	12	223	512	724	ChainA, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_B Chain B, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_C Chain C, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_D Chain D, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_E Chain E, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_F Chain F, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_G Chain G, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10],4KTR_H Chain H, Glycoside hydrolase family 65 central catalytic [[Bacillus] selenitireducens MLS10]
3WIQ_A	1.36e-24	12	227	523	733	Crystalstructure of kojibiose phosphorylase complexed with kojibiose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_A Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_B Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_C Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903],3WIR_D Crystal structure of kojibiose phosphorylase complexed with glucose [Caldicellulosiruptor saccharolyticus DSM 8903]
1H54_A	3.71e-19	13	226	521	728	ChainA, Maltose Phosphorylase [Levilactobacillus brevis],1H54_B Chain B, Maltose Phosphorylase [Levilactobacillus brevis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A9KT32	3.68e-77	1	233	504	751	Nigerose phosphorylase OS=Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) OX=357809 GN=Cphy_1874 PE=1 SV=1
D6XZ22	7.65e-37	12	223	512	724	1,2-alpha-glucosylglycerol phosphorylase OS=Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10) OX=439292 GN=Bsel_2816 PE=1 SV=1
Q8RBL8	3.51e-29	12	232	538	751	Kojibiose phosphorylase OS=Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) OX=273068 GN=kojP PE=3 SV=1
Q8L163	7.60e-28	12	232	541	765	Kojibiose phosphorylase OS=Thermoanaerobacter brockii OX=29323 GN=kojP PE=1 SV=1
Q8L164	1.88e-23	1	233	527	752	Alpha,alpha-trehalose phosphorylase OS=Thermoanaerobacter brockii OX=29323 GN=treP PE=1 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
1.000076	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002713_01934.