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CAZyme Information: MGYG000001553_00702

You are here: Home > Sequence: MGYG000001553_00702

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 Clostridium_P mediterraneense
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_P; Clostridium_P mediterraneense
CAZyme ID MGYG000001553_00702
CAZy Family GH170
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
364 MGYG000001553_5|CGC1 41533.35 5.6449
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001553 3045114 Isolate not provided not provided
Gene Location Start: 302797;  End: 303891  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001553_00702.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH170 3 359 2e-128 0.9942857142857143

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3589 COG3589 5.58e-146 1 363 1 360
Uncharacterized protein [Function unknown].
pfam19200 DUF871_N 7.56e-129 4 240 1 235
DUF871 N-terminal domain. This family consists of several conserved hypothetical proteins from bacteria and archaea. The function of this family is unknown.
pfam05913 DUF871 3.85e-51 246 359 1 115
Bacterial protein of unknown function (DUF871). This family consists of several conserved hypothetical proteins from bacteria and archaea. The function of this family is unknown.
cd00551 AmyAc_family 0.009 49 100 75 118
Alpha amylase catalytic domain family. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; and C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost this catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AQM59666.1 1.30e-207 1 363 1 363
AIY83599.1 7.52e-207 1 363 1 363
QSW20315.1 2.27e-201 1 363 1 363
QAA31287.1 5.14e-200 1 363 1 362
AIY80673.1 7.48e-198 4 359 4 359

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1X7F_A 1.33e-130 2 357 27 381
Crystalstructure of an uncharacterized B. cereus protein [Bacillus cereus ATCC 14579]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A0A0H2XHV5 7.20e-16 5 361 3 345
6-phospho-N-acetylmuramidase OS=Staphylococcus aureus (strain USA300) OX=367830 GN=mupG 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
1.000060 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001553_00702.