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CAZyme Information: MGYG000002414_05801

You are here: Home > Sequence: MGYG000002414_05801

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Paenibacillus odorifer
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus odorifer
CAZyme ID MGYG000002414_05801
CAZy Family GH65
CAZyme Description Phosphoglycolate phosphatase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1001 MGYG000002414_1|CGC122 112737.66 5.2309
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002414 6802552 Isolate South Korea Asia
Gene Location Start: 6521901;  End: 6524906  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.64

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH65 340 714 6.1e-148 0.989247311827957

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG1554 ATH1 0.0 13 773 6 760
Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
PRK13807 PRK13807 0.0 17 781 9 756
maltose phosphorylase; Provisional
pfam03632 Glyco_hydro_65m 5.99e-149 340 719 1 387
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.
pfam03636 Glyco_hydro_65N 9.29e-78 25 283 5 240
Glycosyl hydrolase family 65, N-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. This domain is believed to be essential for catalytic activity although its precise function remains unknown.
TIGR01990 bPGM 1.88e-75 789 973 1 185
beta-phosphoglucomutase. This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AWV36280.1 0.0 1 1001 1 1001
AIQ76999.1 0.0 1 1001 1 1001
AIQ38377.1 0.0 1 1000 22 1021
AIQ26541.1 0.0 12 1000 1 989
AIQ71517.1 0.0 3 999 1 997

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1H54_A 5.76e-120 12 764 4 741
ChainA, Maltose Phosphorylase [Levilactobacillus brevis],1H54_B Chain B, Maltose Phosphorylase [Levilactobacillus brevis]
3WIQ_A 5.75e-118 16 752 6 734
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]
4KTP_A 2.07e-84 18 755 14 732
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 3.94e-84 18 755 14 732
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]
3NAS_A 3.88e-48 787 998 2 215
Thecrystal structure of beta-phosphoglucomutase from Bacillus subtilis [Bacillus subtilis],3NAS_B The crystal structure of beta-phosphoglucomutase from Bacillus subtilis [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8L164 1.05e-263 12 766 9 761
Alpha,alpha-trehalose phosphorylase OS=Thermoanaerobacter brockii OX=29323 GN=treP PE=1 SV=1
Q8GRC3 2.66e-216 18 782 3 758
Alpha,alpha-trehalose phosphorylase OS=Geobacillus stearothermophilus OX=1422 GN=treP PE=1 SV=1
P9WN13 1.09e-168 12 778 6 755
Uncharacterized glycosyl hydrolase Rv3401 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv3401 PE=1 SV=1
P9WN12 1.09e-168 12 778 6 755
Uncharacterized glycosyl hydrolase MT3509 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT3509 PE=3 SV=1
Q49736 7.22e-168 12 778 6 755
Uncharacterized glycosyl hydrolase ML0392 OS=Mycobacterium leprae (strain TN) OX=272631 GN=ML0392 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.999993 0.000043 0.000002 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002414_05801.