CAZyme Information: MGYG000001543_03864

Basic Information

• Species: Lachnoclostridium sp900078195
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnoclostridium; Lachnoclostridium sp900078195
• CAZyme ID: MGYG000001543_03864
• CAZy Family: CE12
• CAZyme Description: Rhamnogalacturonan acetylesterase RhgT

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
239	MGYG000001543_7|CGC31	27006.56	5.3691

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001543	4599950	Isolate	not provided	not provided

• Gene Location: Start: 2513198; End: 2513917 Strand: +

Full Sequence      

MTQKIFWAGDSTVKQNDYTSYPQTGIGQGFLLYMKKDIQMINKAENGRSTKSFIDEGILN
SIDEEIGKDDFLFIQFGHNDEKPDEERHTDAFGSYQENLRKFVDVARKHGAHPVLITSLY
RRLFKEDGTLVDGTHQDYPQAMINLGKELEVPVIDLCSISKDYIQELGDEKSKPLFMHLE
KGAYPNYADGKVDNTHLQYAGAVAFAGIIANELRKLGGIYANILLPLNIKKENPSLLKD

Enzyme Prediction     

No EC number prediction in MGYG000001543_03864.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE12	4	213	7.7e-74	0.9952380952380953

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd01821	Rhamnogalacturan_acetylesterase_like	4.74e-92	3	213	1	198	Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.
COG2755	TesA	8.01e-14	1	218	7	213	Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
cd00229	SGNH_hydrolase	1.76e-06	5	211	1	186	SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.
cd01838	Isoamyl_acetate_hydrolase_like	2.87e-06	64	163	59	169	Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the Saccharomyces cerevisiae IAH1. IAH1 may be the major esterase that hydrolyses isoamyl acetate in sake mash. The SGNH-family of hydrolases is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases
pfam13472	Lipase_GDSL_2	4.78e-06	42	156	38	147	GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABX43096.1	2.45e-120	1	239	1	239
BCJ96416.1	1.07e-92	1	225	1	225
AGF55423.1	3.33e-89	1	224	1	224
AQR94324.1	3.85e-88	1	224	1	224
QOV20143.1	9.81e-83	4	225	5	227

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31523	2.24e-51	4	217	7	216	Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
O31528	1.07e-32	1	217	1	206	Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000037	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001543_03864.