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CAZyme Information: MGYG000000184_01611

You are here: Home > Sequence: MGYG000000184_01611

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 Blautia_A luti
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A luti
CAZyme ID MGYG000000184_01611
CAZy Family GH130
CAZyme Description 4-O-beta-D-mannosyl-D-glucose phosphorylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
950 MGYG000000184_9|CGC1 106625.96 5.0293
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000184 3628099 Isolate China Asia
Gene Location Start: 46881;  End: 49733  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.281

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH130 48 359 3.4e-86 0.9898648648648649

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd05799 PGM2 0.0 419 945 1 487
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
PTZ00150 PTZ00150 1.15e-145 395 950 18 569
phosphoglucomutase-2-like protein; Provisional
COG1109 ManB 7.31e-122 415 950 3 463
Phosphomannomutase [Carbohydrate transport and metabolism].
cd08993 GH130 2.08e-94 65 355 2 278
Glycosyl hydrolase family 130. This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), among others that have yet to be characterized. They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor. This family includes Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) and beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2), enzymes that phosphorolyze beta-mannosidic linkages at the non-reducing ends of their substrates, and have substantially diverse substrate specificity that are determined by three loop regions.
cd05800 PGM_like2 6.86e-85 421 950 2 460
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QJU14271.1 2.29e-236 1 383 1 383
QQQ93190.1 1.85e-235 1 383 1 383
ASU28436.1 1.85e-235 1 383 1 383
ANU75633.1 1.85e-235 1 383 1 383
VCV21228.1 1.55e-224 1 383 1 383

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5AY9_A 5.87e-191 1 383 1 382
Crystalstructure of Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) [Ruminococcus albus 7 = DSM 20455],5AYC_A Crystal structure of Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) in complexes with sulfate and 4-O-beta-D-mannosyl-D-glucose [Ruminococcus albus 7 = DSM 20455]
3WAS_A 1.33e-160 14 383 16 385
Crystalstructure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with Man-Glc+PO4 [Bacteroides fragilis NCTC 9343],3WAS_B Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with Man-Glc+PO4 [Bacteroides fragilis NCTC 9343],3WAT_A Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with Man+Glc [Bacteroides fragilis NCTC 9343],3WAT_B Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with Man+Glc [Bacteroides fragilis NCTC 9343],3WAU_A Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with M1P [Bacteroides fragilis NCTC 9343],3WAU_B Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with M1P [Bacteroides fragilis NCTC 9343],4KMI_A Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with PO4 [Bacteroides fragilis NCTC 9343],4KMI_B Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with PO4 [Bacteroides fragilis NCTC 9343]
1VKD_A 3.25e-27 48 359 37 333
Crystalstructure of a predicted glycosidase (tm1225) from thermotoga maritima msb8 at 2.10 A resolution [Thermotoga maritima MSB8],1VKD_B Crystal structure of a predicted glycosidase (tm1225) from thermotoga maritima msb8 at 2.10 A resolution [Thermotoga maritima MSB8],1VKD_C Crystal structure of a predicted glycosidase (tm1225) from thermotoga maritima msb8 at 2.10 A resolution [Thermotoga maritima MSB8],1VKD_D Crystal structure of a predicted glycosidase (tm1225) from thermotoga maritima msb8 at 2.10 A resolution [Thermotoga maritima MSB8],1VKD_E Crystal structure of a predicted glycosidase (tm1225) from thermotoga maritima msb8 at 2.10 A resolution [Thermotoga maritima MSB8],1VKD_F Crystal structure of a predicted glycosidase (tm1225) from thermotoga maritima msb8 at 2.10 A resolution [Thermotoga maritima MSB8]
1WQA_A 1.50e-25 422 947 5 454
CrystalStructure of Pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with Mg2+ [Pyrococcus horikoshii],1WQA_B Crystal Structure of Pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with Mg2+ [Pyrococcus horikoshii],1WQA_C Crystal Structure of Pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with Mg2+ [Pyrococcus horikoshii],1WQA_D Crystal Structure of Pyrococcus horikoshii phosphomannomutase/phosphoglucomutase complexed with Mg2+ [Pyrococcus horikoshii]
1TUO_A 4.22e-20 420 925 12 442
Crystalstructure of putative phosphomannomutase from Thermus Thermophilus HB8 [Thermus thermophilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P18159 1.21e-192 379 949 1 570
Phosphoglucomutase OS=Bacillus subtilis (strain 168) OX=224308 GN=pgcA PE=1 SV=3
E6UIS7 3.21e-190 1 383 1 382
4-O-beta-D-mannosyl-D-glucose phosphorylase OS=Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7) OX=697329 GN=Rumal_0852 PE=1 SV=1
Q5LH68 7.26e-160 14 383 16 385
4-O-beta-D-mannosyl-D-glucose phosphorylase OS=Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow) OX=272559 GN=BF0772 PE=1 SV=1
Q5HLD2 3.12e-108 410 928 24 527
Phosphoglucomutase OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=pgcA PE=3 SV=1
Q8CN38 4.57e-107 410 928 24 527
Phosphoglucomutase OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=pgcA 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
0.999950 0.000092 0.000004 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000184_01611.