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CAZyme Information: MGYG000000032_03876

You are here: Home > Sequence: MGYG000000032_03876

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 Hungatella effluvii
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Hungatella; Hungatella effluvii
CAZyme ID MGYG000000032_03876
CAZy Family GH65
CAZyme Description Phosphoglycolate phosphatase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
977 MGYG000000032_11|CGC2 109969.21 4.91
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000032 6969476 Isolate United Kingdom Europe
Gene Location Start: 159023;  End: 161956  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.64

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH65 320 692 1e-141 0.9946236559139785

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG1554 ATH1 0.0 4 745 11 756
Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
PRK13807 PRK13807 1.03e-150 9 752 15 751
maltose phosphorylase; Provisional
pfam03632 Glyco_hydro_65m 9.66e-133 320 692 1 384
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.
TIGR01990 bPGM 5.93e-78 767 952 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]
pfam03636 Glyco_hydro_65N 1.56e-62 9 263 3 239
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QIB56130.1 0.0 1 752 1 756
QMW81136.1 0.0 1 752 1 756
QBE96086.1 0.0 1 752 1 756
QJU16469.1 0.0 1 749 1 753
QQQ95359.1 0.0 1 749 1 753

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3WIQ_A 9.39e-97 3 726 7 732
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 6.84e-91 4 753 10 754
ChainA, Maltose Phosphorylase [Levilactobacillus brevis],1H54_B Chain B, Maltose Phosphorylase [Levilactobacillus brevis]
4KTP_A 3.63e-78 19 749 27 752
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 4.99e-78 19 749 27 752
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]
7FE3_A 2.51e-43 242 705 239 659
ChainA, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE3_B Chain B, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE3_C Chain C, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE4_A Chain A, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE4_B Chain B, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101],7FE4_C Chain C, Candidate alpha glycoside phosphorylase Glycoside hydrolase family 65 [Flavobacterium johnsoniae UW101]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GRC3 5.38e-266 16 750 13 750
Alpha,alpha-trehalose phosphorylase OS=Geobacillus stearothermophilus OX=1422 GN=treP PE=1 SV=1
Q8L164 8.17e-186 4 749 15 768
Alpha,alpha-trehalose phosphorylase OS=Thermoanaerobacter brockii OX=29323 GN=treP PE=1 SV=1
P9WN13 4.70e-131 22 742 28 741
Uncharacterized glycosyl hydrolase Rv3401 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv3401 PE=1 SV=1
P9WN12 4.70e-131 22 742 28 741
Uncharacterized glycosyl hydrolase MT3509 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT3509 PE=3 SV=1
Q49736 1.00e-125 22 742 28 741
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
1.000024 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000032_03876.