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CAZyme Information: MGYG000001131_01003

You are here: Home > Sequence: MGYG000001131_01003

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 Prevotella sp900543585
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900543585
CAZyme ID MGYG000001131_01003
CAZy Family GH43
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
693 77326.65 7.2839
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001131 3153631 MAG China Asia
Gene Location Start: 30762;  End: 32843  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001131_01003.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH43 404 670 4.7e-99 0.9925373134328358

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd09019 galactose_mutarotase_like 6.81e-155 60 395 1 326
galactose mutarotase_like. Galactose mutarotase catalyzes the conversion of beta-D-galactose to alpha-D-galactose. Beta-D-galactose is produced by the degradation of lactose, a disaccharide composed of beta-D-glucose and beta-D-galactose. This epimerization reaction is the first step in the four-step Leloir pathway, which converts galactose into metabolically important glucose. This epimerization step is followed by the phosophorylation of alpha-D-galactose by galactokinase, an enzyme which can only act on the alpha anomer. A glutamate and a histidine residue of the galactose mutarotase have been shown to be critical for catalysis, the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. Galactose mutarotase is a member of the aldose-1-epimerase superfamily.
cd08991 GH43_HoAraf43-like 2.35e-113 406 672 1 274
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580). This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
TIGR02636 galM_Leloir 2.30e-111 55 396 1 336
galactose mutarotase. Members of this protein family act as galactose mutarotase (D-galactose 1-epimerase) and participate in the Leloir pathway for galactose/glucose interconversion. All members of the seed alignment for this model are found in gene clusters with other enzymes of the Leloir pathway. This enzyme family belongs to the aldose 1-epimerase family, described by pfam01263. However, the enzyme described as aldose 1-epimerase itself (EC 5.1.3.3) is called broadly specific for D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose. The restricted genome context for genes in this family suggests members should act primarily on D-galactose.
PRK11055 galM 1.91e-102 55 398 6 342
galactose-1-epimerase; Provisional
pfam01263 Aldose_epim 3.37e-81 59 394 1 300
Aldose 1-epimerase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
VEH14885.1 4.52e-201 40 397 339 696
AXV50356.1 1.24e-196 39 399 331 691
QUI92994.1 9.61e-196 39 396 331 688
QUB89410.1 1.92e-195 39 396 331 688
QUB93993.1 1.92e-195 39 396 331 688

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1SNZ_A 3.44e-66 69 398 31 344
Crystalstructure of apo human galactose mutarotase [Homo sapiens],1SNZ_B Crystal structure of apo human galactose mutarotase [Homo sapiens],1SO0_A Crystal structure of human galactose mutarotase complexed with galactose [Homo sapiens],1SO0_B Crystal structure of human galactose mutarotase complexed with galactose [Homo sapiens],1SO0_C Crystal structure of human galactose mutarotase complexed with galactose [Homo sapiens],1SO0_D Crystal structure of human galactose mutarotase complexed with galactose [Homo sapiens]
4RNL_A 3.51e-64 68 397 33 342
Thecrystal structure of a possible galactose mutarotase from Streptomyces platensis subsp. rosaceus [Streptomyces platensis],4RNL_B The crystal structure of a possible galactose mutarotase from Streptomyces platensis subsp. rosaceus [Streptomyces platensis],4RNL_C The crystal structure of a possible galactose mutarotase from Streptomyces platensis subsp. rosaceus [Streptomyces platensis],4RNL_D The crystal structure of a possible galactose mutarotase from Streptomyces platensis subsp. rosaceus [Streptomyces platensis]
3KST_A 3.53e-56 394 665 12 282
Crystalstructure of Endo-1,4-beta-xylanase (NP_811807.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.70 A resolution [Bacteroides thetaiotaomicron VPI-5482],3KST_B Crystal structure of Endo-1,4-beta-xylanase (NP_811807.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.70 A resolution [Bacteroides thetaiotaomicron VPI-5482]
1L7J_A 2.00e-41 55 400 9 341
ChainA, galactose mutarotase [Lactococcus lactis],1L7J_B Chain B, galactose mutarotase [Lactococcus lactis],1L7K_A Chain A, galactose mutarotase [Lactococcus lactis],1L7K_B Chain B, galactose mutarotase [Lactococcus lactis],1MMU_A Chain A, Aldose 1-epimerase [Lactococcus lactis],1MMU_B Chain B, Aldose 1-epimerase [Lactococcus lactis],1MMX_A Chain A, Aldose 1-epimerase [Lactococcus lactis],1MMX_B Chain B, Aldose 1-epimerase [Lactococcus lactis],1MMY_A Chain A, Aldose 1-epimerase [Lactococcus lactis],1MMY_B Chain B, Aldose 1-epimerase [Lactococcus lactis],1MMZ_A Chain A, Aldose 1-epimerase [Lactococcus lactis],1MMZ_B Chain B, Aldose 1-epimerase [Lactococcus lactis],1MN0_A Chain A, Aldose 1-epimerase [Lactococcus lactis],1MN0_B Chain B, Aldose 1-epimerase [Lactococcus lactis]
1NS0_A 5.15e-41 55 400 9 341
ChainA, GALACTOSE MUTAROTASE [Lactococcus lactis],1NS0_B Chain B, GALACTOSE MUTAROTASE [Lactococcus lactis],1NS4_A Chain A, GALACTOSE MUTAROTASE [Lactococcus lactis],1NS4_B Chain B, GALACTOSE MUTAROTASE [Lactococcus lactis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P05149 4.81e-69 55 399 34 381
Aldose 1-epimerase OS=Acinetobacter calcoaceticus OX=471 GN=mro PE=1 SV=1
Q66HG4 1.67e-67 55 398 16 342
Galactose mutarotase OS=Rattus norvegicus OX=10116 GN=Galm PE=1 SV=1
Q8K157 9.14e-66 55 398 16 342
Galactose mutarotase OS=Mus musculus OX=10090 GN=Galm PE=1 SV=1
Q96C23 1.78e-65 69 398 29 342
Galactose mutarotase OS=Homo sapiens OX=9606 GN=GALM PE=1 SV=1
Q5EA79 9.38e-65 66 398 26 342
Galactose mutarotase OS=Bos taurus OX=9913 GN=GALM PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000361 0.998376 0.000700 0.000205 0.000176 0.000167

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001131_01003.