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CAZyme Information: MGYG000000600_01411

You are here: Home > Sequence: MGYG000000600_01411

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 CAG-791 sp000431495
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-791; CAG-791 sp000431495
CAZyme ID MGYG000000600_01411
CAZy Family GH8
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
755 MGYG000000600_19|CGC1 85600.88 4.8119
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000600 2612842 MAG Madagascar Africa
Gene Location Start: 27958;  End: 30225  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.156 3.2.1.8

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH8 418 747 1.9e-76 0.93125

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3405 BcsZ 8.01e-73 411 755 37 351
Endo-1,4-beta-D-glucanase Y [Carbohydrate transport and metabolism].
cd07712 MBLAC2-like_MBL-fold 4.17e-39 72 254 10 182
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain. Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
cd06262 metallo-hydrolase-like_MBL-fold 1.99e-20 67 214 6 147
mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.
smart00849 Lactamase_B 4.69e-20 72 215 1 137
Metallo-beta-lactamase superfamily. Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.
cd07729 AHL_lactonase_MBL-fold 1.74e-18 72 254 33 236
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain. Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNO17280.1 1.13e-165 388 754 26 380
CBL10560.1 2.27e-160 388 755 27 383
CBL13086.1 2.27e-160 388 755 27 383
EEU99943.1 1.16e-157 388 755 27 383
VCV21314.1 1.16e-157 388 755 27 383

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5YXT_A 3.10e-141 385 754 26 375
Glycosidehydrolase family 8 Xylanase [Paenibacillus barengoltzii G22],5YXT_B Glycoside hydrolase family 8 Xylanase [Paenibacillus barengoltzii G22],5YXT_C Glycoside hydrolase family 8 Xylanase [Paenibacillus barengoltzii G22],5YXT_D Glycoside hydrolase family 8 Xylanase [Paenibacillus barengoltzii G22]
1WU4_A 7.86e-137 388 754 30 378
ChainA, xylanase Y [Halalkalibacterium halodurans C-125],1WU5_A Chain A, xylanase Y [Halalkalibacterium halodurans C-125]
3A3V_A 3.12e-136 388 754 30 378
ChainA, Xylanase Y [Halalkalibacterium halodurans]
2DRR_A 4.41e-136 388 754 30 378
ChainA, Xylanase Y [Halalkalibacterium halodurans C-125]
1WU6_A 6.22e-136 388 754 30 378
ChainA, xylanase Y [Halalkalibacterium halodurans C-125]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9KB30 3.28e-136 388 754 30 378
Reducing end xylose-releasing exo-oligoxylanase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=BH2105 PE=1 SV=1
A1A048 5.20e-129 385 753 25 377
Reducing end xylose-releasing exo-oligoxylanase OS=Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) OX=367928 GN=xylA PE=1 SV=1
A0A0S2UQQ5 7.60e-129 389 755 31 380
Reducing-end xylose-releasing exo-oligoxylanase Rex8A OS=Paenibacillus barcinonensis OX=198119 GN=rex8A PE=1 SV=1
P37699 2.74e-18 392 752 68 389
Endoglucanase C OS=Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) OX=394503 GN=celCCC PE=1 SV=2
P37701 3.65e-18 392 752 68 389
Endoglucanase 2 OS=Ruminiclostridium josui OX=1499 GN=celB 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
1.000052 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000600_01411.