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CAZyme Information: MGYG000004223_00350

You are here: Home > Sequence: MGYG000004223_00350

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 UMGS1883 sp900763305
Lineage Bacteria; Firmicutes_A; Clostridia; UMGS1883; UMGS1883; UMGS1883; UMGS1883 sp900763305
CAZyme ID MGYG000004223_00350
CAZy Family GH65
CAZyme Description Phosphoglycolate phosphatase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1064 MGYG000004223_2|CGC3 119746.49 5.5994
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004223 2575981 MAG United Kingdom Europe
Gene Location Start: 156143;  End: 159337  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004223_00350.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH65 405 780 3.8e-130 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 97 845 6 768
Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
PRK13807 PRK13807 1.78e-156 98 841 6 752
maltose phosphorylase; Provisional
pfam03632 Glyco_hydro_65m 1.34e-118 405 783 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.
TIGR01990 bPGM 2.25e-88 859 1042 1 184
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]
TIGR02009 PGMB-YQAB-SF 2.06e-71 858 1040 2 183
beta-phosphoglucomutase family hydrolase. This subfamily model groups together three clades: the characterized beta-phosphoglucomutases (including those from E.coli, B.subtilus and L.lactis, TIGR01990), a clade of putative bPGM's from mycobacteria and a clade including the uncharacterized E.coli and H.influenzae yqaB genes which may prove to be beta-mutases of a related 1-phosphosugar. All of these are members of the larger Haloacid dehalogenase (HAD) subfamily IA and include the "variant 3" glu-asp version of the third conserved HAD domain (TIGR01509).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AVX19567.1 1.49e-227 97 1037 10 962
ALS24964.1 8.63e-227 94 1042 7 957
QQE76864.1 9.12e-227 94 1042 16 974
AVX29984.1 2.60e-225 97 1037 10 962
AZK48442.1 6.29e-224 85 1045 3 976

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3WIQ_A 9.10e-91 105 823 10 743
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 1.66e-87 97 834 5 747
ChainA, Maltose Phosphorylase [Levilactobacillus brevis],1H54_B Chain B, Maltose Phosphorylase [Levilactobacillus brevis]
4KTP_A 7.73e-86 99 840 9 755
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 1.47e-85 99 840 9 755
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]
4GIB_A 1.38e-43 853 1037 22 208
ChainA, Beta-phosphoglucomutase [Clostridioides difficile 630],4GIB_B Chain B, Beta-phosphoglucomutase [Clostridioides difficile 630]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8L164 2.58e-181 106 838 19 769
Alpha,alpha-trehalose phosphorylase OS=Thermoanaerobacter brockii OX=29323 GN=treP PE=1 SV=1
Q8GRC3 1.95e-122 109 833 10 745
Alpha,alpha-trehalose phosphorylase OS=Geobacillus stearothermophilus OX=1422 GN=treP PE=1 SV=1
Q8RBL8 4.24e-105 115 837 29 771
Kojibiose phosphorylase OS=Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) OX=273068 GN=kojP PE=3 SV=1
O06993 1.08e-99 97 837 7 746
Maltose phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=mdxK PE=3 SV=1
P9WN13 7.66e-98 106 840 16 753
Uncharacterized glycosyl hydrolase Rv3401 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv3401 PE=1 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
1.000050 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004223_00350.