dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

RC9 sp900767375

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp900767375

CAZyme ID

MGYG000003445_01439

CAZy Family

GH43

CAZyme Description

Hydroxyacylglutathione hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
937		103599.35	5.7883

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003445	1789928	MAG	Fiji	Oceania

Gene Location

Start: 7393; End: 10206 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000003445_01439.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH43	24	361	3.3e-109	0.9965986394557823

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18620	GH43_XylA-like	2.34e-70	34	364	1	269	Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium alpha-L-arabinofuranosidase XylA. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) 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. The GH43_XylA-like subgroup includes Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and enzymes that have been annotated as having beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), endo-alpha-L-arabinanase (EC 3.2.1.-) as well as arabinoxylan arabinofuranohydrolase (AXH) 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. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan.
cd07712	MBLAC2-like_MBL-fold	4.56e-42	708	867	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.
cd08990	GH43_AXH_like	2.14e-29	35	364	2	264	Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, beta-xylosidase, endo-1,4-beta-xylanase, and alpha-L-arabinofuranosidase. This subgroup includes Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160), Butyrivibrio proteoclasticus alpha-L-arabinofuranosidase (Xsa43E;bpr_I2319), Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and metagenomic beta-xylosidase (EC 3.2.1.37) / alpha-L-arabinofuranosidase (EC 3.2.1.55) CoXyl43. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_AXH-like subgroup includes enzymes that have been characterized with beta-xylosidase, alpha-L-arabinofuranosidase, endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) 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. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43 shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. 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.
cd06262	metallo-hydrolase-like_MBL-fold	1.32e-25	710	867	13	188	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	3.59e-25	710	867	3	177	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNL41333.1	0.0	24	667	36	681
QCD37057.1	0.0	24	667	30	675
QRQ49698.1	3.51e-316	24	674	41	692
QUT44391.1	1.22e-315	24	674	56	707
ALJ60075.1	1.53e-315	24	667	42	688

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NOV_A	2.11e-13	35	365	56	328	Xsa43E,a GH43 family enzyme from Butyrivibrio proteoclasticus [Butyrivibrio proteoclasticus B316]
4AD9_A	4.54e-06	710	867	35	200	Crystalstructure of human LACTB2. [Homo sapiens],4AD9_B Crystal structure of human LACTB2. [Homo sapiens],4AD9_C Crystal structure of human LACTB2. [Homo sapiens],4AD9_D Crystal structure of human LACTB2. [Homo sapiens],4AD9_E Crystal structure of human LACTB2. [Homo sapiens],4AD9_F Crystal structure of human LACTB2. [Homo sapiens]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P48790	4.23e-31	24	469	7	404	Xylosidase/arabinosidase OS=Thermoclostridium stercorarium OX=1510 GN=xylA PE=1 SV=1
Q5F336	3.33e-11	699	879	13	240	Acyl-coenzyme A thioesterase MBLAC2 OS=Gallus gallus OX=9031 GN=MBLAC2 PE=2 SV=1
Q68D91	2.11e-09	699	879	13	243	Acyl-coenzyme A thioesterase MBLAC2 OS=Homo sapiens OX=9606 GN=MBLAC2 PE=1 SV=3
Q8BL86	2.11e-09	719	879	62	243	Acyl-coenzyme A thioesterase MBLAC2 OS=Mus musculus OX=10090 GN=Mblac2 PE=1 SV=2
A5PJT0	3.80e-09	699	879	13	243	Acyl-coenzyme A thioesterase MBLAC2 OS=Bos taurus OX=9913 GN=MBLAC2 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
0.000290	0.998986	0.000224	0.000168	0.000153	0.000142

TMHMM Annotations help

There is no transmembrane helices in MGYG000003445_01439.

You are here: Home > Sequence: MGYG000003445_01439