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CAZyme Information: MGYG000000473_00715

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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 UBA10281 sp900767495
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; UBA10281; UBA10281 sp900767495
CAZyme ID MGYG000000473_00715
CAZy Family GH95
CAZyme Description Phosphoglycolate phosphatase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
972 MGYG000000473_23|CGC2 108927.85 5.5012
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000473 1843328 MAG Fiji Oceania
Gene Location Start: 17552;  End: 20470  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000473_00715.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH95 222 948 7.7e-179 0.9736842105263158

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR01990 bPGM 2.77e-74 4 188 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 (, trehalose ( or trehalose-6-phosphate ( 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 2.50e-60 2 186 1 184
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).
cd02598 HAD_BPGM 3.64e-49 4 206 1 166
beta-phosphoglucomutase, similar to Lactococcus lactis beta-phosphoglucomutase (beta-PGM). Lactococcus lactis beta-PGM catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate as an intermediate. In the forward G6P-forming direction, this reaction links polysaccharide phosphorolysis to glycolysis, in the reverse direction, the reaction provides G1P for the biosynthesis of exo-polysaccharides. This subfamily belongs to the beta-phosphoglucomutase-like family whose other members include Saccharomyces cerevisiae phosphatases GPP1 and GPP2 that dephosphorylate DL-glycerol-3-phosphate and DOG1 and DOG2 that dephosphorylate 2-deoxyglucose-6-phosphate, and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.
COG0637 YcjU 3.97e-45 1 213 1 219
Beta-phosphoglucomutase or related phosphatase, HAD superfamily [Carbohydrate transport and metabolism, General function prediction only].
pfam14498 Glyco_hyd_65N_2 1.08e-30 222 453 3 233
Glycosyl hydrolase family 65, N-terminal domain. This domain represents a domain found to the N-terminus of the glycosyl hydrolase 65 family catalytic domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AHW58797.1 2.72e-119 222 945 30 751
QIA08082.1 3.94e-118 222 959 30 761
QDH81513.1 3.89e-115 212 951 22 763
BBE15989.1 1.21e-114 222 945 30 752
ADX05719.1 1.39e-114 235 960 50 760

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4UFC_A 4.85e-100 235 945 36 741
Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus]
7KMQ_A 1.42e-97 235 950 55 762
ChainA, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306],7KMQ_B Chain B, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306]
2RDY_A 8.41e-82 222 960 7 765
ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125]
2EAB_A 1.12e-55 236 949 52 855
Crystalstructure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAB_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAC_A Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum],2EAC_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum]
2EAD_A 6.53e-55 236 949 52 855
ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8L7W8 2.99e-89 235 938 66 805
Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1
A2R797 3.75e-65 223 933 26 765
Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1
Q5AU81 1.92e-51 239 921 47 772
Alpha-fucosidase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=afcA PE=1 SV=1
O06995 4.68e-41 3 217 2 217
Beta-phosphoglucomutase OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdM PE=1 SV=1
Q2USL3 3.77e-40 235 945 32 714
Probable alpha-fucosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=afcA PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

1.000027 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000473_00715.