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CAZyme Information: MGYG000004439_00366

You are here: Home > Sequence: MGYG000004439_00366

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
Lineage Bacteria; Firmicutes_A; Clostridia; UMGS1810; UMGS1810; ;
CAZyme ID MGYG000004439_00366
CAZy Family GH57
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
734 82085.84 4.7251
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004439 2174785 MAG Israel Asia
Gene Location Start: 33779;  End: 35983  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004439_00366.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH57 280 426 1.5e-20 0.4308093994778068

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10794 GH57N_PfGalA_like 2.30e-81 278 615 1 305
N-terminal catalytic domain of alpha-galactosidase; glycoside hydrolase family 57 (GH57). Alpha-galactosidases (GalA, EC 3.2.1.22) catalyze the hydrolysis of alpha-1,6-linked galactose residues from oligosaccharides and polymeric galactomannans. Based on sequence similarity, the majority of eukaryotic and bacterial GalAs have been classified into glycoside hydrolase family GH27, GH36, and GH4, respectively. This subfamily is represented by a novel type of GalA from Pyrococcus furiosus (PfGalA), which belongs to the GH57 family. PfGalA is an extremely thermo-active and thermostable GalA that functions as a bacterial-like GalA, however, without the capacity to hydrolyze polysaccharides. It specifically catalyzes the hydrolysis of para-nitrophenyl-alpha-galactopyranoside, and to some extent that of melibiose and raffinose. PfGalA has a pH optimum between 5.0-5.5.
pfam01261 AP_endonuc_2 4.12e-19 19 260 1 240
Xylose isomerase-like TIM barrel. This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.
COG1082 YcjR 5.13e-18 1 265 3 268
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism].
cd01022 GH57N_like 5.11e-13 277 421 2 166
N-terminal catalytic domain of heat stable retaining glycoside hydrolase family 57. Glycoside hydrolase family 57(GH57) is a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57s cleave alpha-glycosidic bonds by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation.
pfam03065 Glyco_hydro_57 1.22e-12 259 424 12 179
Glycosyl hydrolase family 57. This family includes alpha-amylase (EC:3.2.1.1), 4--glucanotransferase (EC:2.4.1.-) and amylopullulanase enzymes.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AVM45997.1 2.90e-236 274 734 4 459
AHF90539.1 3.64e-204 278 734 7 463
QDT00377.1 8.66e-47 282 730 8 438
BCW88139.1 1.01e-14 282 419 26 162
QAZ69632.1 6.69e-14 276 420 2 146

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      help

has no Swissprot hit.

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
1.000040 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004439_00366.