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CAZyme Information: MGYG000000128_01279

You are here: Home > Sequence: MGYG000000128_01279

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 Alistipes sp902363575
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp902363575
CAZyme ID MGYG000000128_01279
CAZy Family GH65
CAZyme Description Phosphoglycolate phosphatase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
984 MGYG000000128_2|CGC5 110032.7 5.8134
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000128 2906288 Isolate Canada North America
Gene Location Start: 569138;  End: 572092  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.8

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH65 540 920 1.6e-143 0.9946236559139785

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK13807 PRK13807 0.0 229 982 1 754
maltose phosphorylase; Provisional
COG1554 ATH1 0.0 231 971 4 755
Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism].
pfam03632 Glyco_hydro_65m 8.28e-166 540 923 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 6.88e-76 6 190 3 185
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]
TIGR02009 PGMB-YQAB-SF 9.41e-65 2 189 1 185
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
CBK62951.1 0.0 229 981 2 755
QKG79963.1 1.64e-312 232 976 4 759
QNR25625.1 1.18e-311 229 971 2 756
AFD07362.1 1.93e-308 231 977 3 759
QHL86664.1 2.13e-307 231 966 3 741

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1H54_A 3.17e-216 231 980 3 754
ChainA, Maltose Phosphorylase [Levilactobacillus brevis],1H54_B Chain B, Maltose Phosphorylase [Levilactobacillus brevis]
3WIQ_A 2.09e-101 254 971 22 751
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 1.78e-67 237 961 13 734
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 3.30e-67 237 961 13 734
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 3.94e-46 6 216 6 216
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
O06993 1.99e-235 229 956 3 725
Maltose phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=mdxK PE=3 SV=1
E6ENP7 5.46e-231 231 981 25 773
Maltose phosphorylase OS=Enterococcus faecalis (strain TX4000 / JH2-2) OX=749493 GN=malP PE=1 SV=1
Q8L164 2.01e-125 236 967 13 759
Alpha,alpha-trehalose phosphorylase OS=Thermoanaerobacter brockii OX=29323 GN=treP PE=1 SV=1
Q8RBL8 1.87e-99 238 958 16 751
Kojibiose phosphorylase OS=Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) OX=273068 GN=kojP PE=3 SV=1
Q8GRC3 6.07e-99 238 958 3 730
Alpha,alpha-trehalose phosphorylase OS=Geobacillus stearothermophilus OX=1422 GN=treP 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
1.000080 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000128_01279.