CAZyme Information: MGYG000002381_02382

Basic Information

• Species: Stenotrophomonas bentonitica_A
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas bentonitica_A
• CAZyme ID: MGYG000002381_02382
• CAZy Family: CE12
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
367		40050.49	6.8829

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002381	4114425	Isolate	not provided	not provided

• Gene Location: Start: 42484; End: 43587 Strand: -

Full Sequence      

MLRLLLSLSFLLAAPSALCAPHRIFIAGDSTAAEYGPERAPQAGWGQALQSYLDPAVWEV
RNHAKGGRSTRSFIDEKRLDAIAAELQRGDVLLIQFGHNDAKFEDPTRYTDPAVAYPRFL
MRYVQLARDKGATPVLITPVARLLYDFGSLLDTHGVYTQAVKALASREQVALIDLNDSST
RWIRGLGEQGARPYFMFVPEQNKADGTHFSVAGATAVACLVMRDWVALQPELTSALKRDI
DCEVRSAGRGGEATKPSRVVHERDIAVTQPGPHGGAGPTTAYPFFAEDTDLPFVLRKRVL
HKGAGIGLHPQHKDEIYYIVSGQGSYVLDGKQYDVAAGDALLTKTGSSHALQQVGEEDLV
VLLAYPR

Enzyme Prediction     

No EC number prediction in MGYG000002381_02382.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE12	23	223	2.5e-68	0.9857142857142858

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd01821	Rhamnogalacturan_acetylesterase_like	1.14e-82	23	221	2	194	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.
cd02221	cupin_TM1287-like	5.42e-26	277	362	1	89	Thermotoga maritima TM1287 decarboxylase, cupin domain. This family includes bacterial proteins homologous to TM1287 decarboxylase, a Thermotoga maritima manganese-containing cupin thought to catalyze the conversion of oxalate to formate and carbon dioxide, due to its similarity to oxalate decarboxylase (OXDC) from Bacillus subtilis. TM1287 shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer.
COG2755	TesA	8.88e-25	20	218	7	201	Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
cd00229	SGNH_hydrolase	9.72e-14	24	218	1	181	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.
pfam07883	Cupin_2	2.37e-11	299	365	4	70	Cupin domain. This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOX62470.1	3.08e-265	1	367	1	367
QHB73410.1	3.62e-248	1	367	1	367
AHY60924.1	5.78e-247	2	367	1	366
QIO86378.1	1.38e-239	1	367	3	370
AOA70603.1	3.27e-226	3	367	3	368

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2O14_A	7.02e-21	24	224	165	358	X-RayCrystal Structure of Protein YXIM_BACsu from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR595 [Bacillus subtilis]
1DEO_A	1.30e-13	24	236	3	223	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	6.02e-13	24	236	3	223	ChainA, Rhamnogalacturonan acetylesterase [Aspergillus aculeatus]
1O4T_A	2.74e-07	288	362	40	127	Crystalstructure of a predicted oxalate decarboxylase (tm1287) from thermotoga maritima at 1.95 A resolution [Thermotoga maritima],1O4T_B Crystal structure of a predicted oxalate decarboxylase (tm1287) from thermotoga maritima at 1.95 A resolution [Thermotoga maritima]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31528	5.65e-44	22	239	3	216	Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
O31523	5.50e-41	21	221	5	208	Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
P42304	1.86e-21	24	224	180	373	Uncharacterized esterase YxiM OS=Bacillus subtilis (strain 168) OX=224308 GN=yxiM PE=1 SV=2
Q5BAA2	7.26e-14	5	243	6	243	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	3.63e-13	15	236	13	240	Rhamnogalacturonan acetylesterase OS=Aspergillus aculeatus OX=5053 GN=rha1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000264	0.999136	0.000163	0.000150	0.000137	0.000131

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002381_02382.