dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: HUMAN GUT

help

CAZyme Information: MGYG000002424_02241

You are here: Home > Sequence: MGYG000002424_02241

Basic Information help

Species

Monoglobus pectinilyticus

Lineage

Bacteria; Firmicutes_A; Clostridia; Monoglobales; Monoglobaceae; Monoglobus; Monoglobus pectinilyticus

CAZyme ID

MGYG000002424_02241

CAZy Family

CE12

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
867	MGYG000002424_1\|CGC31	94257.79	4.4575

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002424	2757122	Isolate	New Zealand	Oceania

Gene Location

Start: 2673818; End: 2676421 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002424_02241.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CE12	595	838	1.1e-56	0.9952380952380953

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd01821	Rhamnogalacturan_acetylesterase_like	1.79e-52	595	788	2	189	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	1.48e-10	588	753	3	172	Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
cd00229	SGNH_hydrolase	5.18e-06	596	762	1	163	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.
pfam00657	Lipase_GDSL	2.02e-05	596	762	1	199	GDSL-like Lipase/Acylhydrolase.
pfam13472	Lipase_GDSL_2	3.40e-05	600	753	3	148	GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUO20372.1	0.0	1	867	1	867
AUO20219.1	1.46e-49	596	839	125	351
ARK29532.1	3.89e-36	596	832	6	207
AGC68045.1	2.93e-34	596	845	8	221
ANW98437.1	2.93e-34	596	845	8	221

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2O14_A	2.39e-11	593	772	162	335	X-RayCrystal Structure of Protein YXIM_BACsu from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR595 [Bacillus subtilis]
5HO0_A	3.94e-10	380	475	548	645	Crystalstructure of AbnA (closed conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HO2_A Crystal structure of AbnA (open conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HOF_A Crystal structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinopentaose [Geobacillus stearothermophilus],5HP6_A Structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus (a new conformational state) [Geobacillus stearothermophilus]
5HO9_A	5.83e-10	380	469	548	639	Structureof truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus],5HO9_B Structure of truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus]
1DEO_A	1.37e-07	595	675	2	75	RHAMNOGALACTURONANACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.55 A RESOLUTION WITH SO4 IN THE ACTIVE SITE [Aspergillus aculeatus],1DEX_A RHAMNOGALACTURONAN ACETYLESTERASE FROM ASPERGILLUS ACULEATUS AT 1.9 A RESOLUTION [Aspergillus aculeatus],1K7C_A Rhamnogalacturonan acetylesterase with seven N-linked carbohydrate residues distributed at two N-glycosylation sites refined at 1.12 A resolution [Aspergillus aculeatus],1PP4_A The crystal structure of rhamnogalacturonan acetylesterase in space group P3121 [Aspergillus aculeatus],1PP4_B The crystal structure of rhamnogalacturonan acetylesterase in space group P3121 [Aspergillus aculeatus]
3C1U_A	1.37e-07	595	675	2	75	ChainA, Rhamnogalacturonan acetylesterase [Aspergillus aculeatus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31523	1.54e-27	596	845	8	219	Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
O31528	5.55e-18	596	767	5	169	Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
P42304	7.84e-12	593	772	177	350	Uncharacterized esterase YxiM OS=Bacillus subtilis (strain 168) OX=224308 GN=yxiM PE=1 SV=2
Q5BAA2	6.99e-10	595	766	19	195	Rhamnogalacturonan acetylesterase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=AN2528 PE=1 SV=1
Q00017	9.04e-07	595	675	19	92	Rhamnogalacturonan acetylesterase OS=Aspergillus aculeatus OX=5053 GN=rha1 PE=1 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
0.002008	0.996776	0.000561	0.000240	0.000196	0.000187

TMHMM Annotations download full data without filtering help

start	end
7	29