CAZyme Information: MGYG000000574_00166

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae
• CAZyme ID: MGYG000000574_00166
• CAZy Family: GH65
• CAZyme Description: Maltose phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
220	MGYG000000574_11|CGC1	25536.88	5.8889

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000574	5306470	MAG	Madagascar	Africa

• Gene Location: Start: 11723; End: 12385 Strand: -

Full Sequence      

MERDGVAHVYSSLPHVDVDAIPVADFPLYEHWSYDRIYRNDMVKQPDVLMFFLMFPSGFT
GEQLRRNYEYYEPRCIHESSLSPSVHSILASRLKKHKEAYEFFRFATRMDLDNYNRNTRE
GLHTTSIAAAWMNIVYGFGGMQSDGACLSLSPSIPEQWQSYSFRLGYQEDIIVVEVGRET
VSLYTLNGKNIRIWLYKEEVVLGKEVLSRRMCDGDESTGK

Enzyme Prediction     

No EC number prediction in MGYG000000574_00166.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH65	10	143	3.4e-46	0.3575268817204301

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK13807	PRK13807	1.50e-72	18	206	564	752	maltose phosphorylase; Provisional
COG1554	ATH1	1.25e-60	10	202	565	760	Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
pfam03632	Glyco_hydro_65m	1.15e-50	10	145	246	384	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.
pfam03633	Glyco_hydro_65C	7.90e-10	152	201	1	50	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLY80560.1	3.45e-99	10	208	560	758
ABX43668.1	6.92e-95	10	207	602	799
BCK00435.1	2.40e-89	10	207	561	758
SET84823.1	3.87e-87	10	205	561	756
AIQ48384.1	5.08e-84	2	214	556	764

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1H54_A	3.23e-40	18	193	566	741	ChainA, Maltose Phosphorylase [Levilactobacillus brevis],1H54_B Chain B, Maltose Phosphorylase [Levilactobacillus brevis]
4KTP_A	1.74e-28	39	209	582	759	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	1.74e-28	39	209	582	759	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	8.12e-26	35	203	587	757	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O06993	8.82e-53	18	202	562	746	Maltose phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=mdxK PE=3 SV=1
E6ENP7	4.04e-47	16	202	577	768	Maltose phosphorylase OS=Enterococcus faecalis (strain TX4000 / JH2-2) OX=749493 GN=malP PE=1 SV=1
Q8L164	1.62e-44	16	204	582	770	Alpha,alpha-trehalose phosphorylase OS=Thermoanaerobacter brockii OX=29323 GN=treP PE=1 SV=1
Q8GRC3	1.38e-34	17	205	564	752	Alpha,alpha-trehalose phosphorylase OS=Geobacillus stearothermophilus OX=1422 GN=treP PE=1 SV=1
Q8RBL8	1.48e-30	40	202	607	771	Kojibiose phosphorylase OS=Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) OX=273068 GN=kojP 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
1.000025	0.000008	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000574_00166.