CAZyme Information: MGYG000003515_00315

Basic Information

• Species: Prevotella sp900769275
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900769275
• CAZyme ID: MGYG000003515_00315
• CAZy Family: CE12
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
614		69747.65	8.8484

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003515	2052370	MAG	Fiji	Oceania

• Gene Location: Start: 1864; End: 3708 Strand: -

Full Sequence      

MKILTTLTIYLALASLSANAQNNNEQGDIWIDINGVRDLTADSIDIANQARPVSGSSRKG
DNPVIFLVGNSTMRTGTRGNGDNGQWGWGYYEHEYYDADKVTVENHALGGTSPRTFYKSP
DLWQRTIAGLRKGDYVFLELGHNDNGPIDEIRARSSYRPHGKLSLAEDSVIIYNKVKQCQ
DTVYTFGGYTRRFINEVRQRGAIPVLFTLTPRNDYEVDGKTIQRKLKDFTPAIFAIGKEM
NVPVVDLNDISARKLETYGKWKTNYHFYLDKIHSSAFGARMNAESAAEGILCLNLDDNTA
LNTSDSLFLVEKEALLRLKSYLIKDKVCPDYEEKLLAWEPDNYDAQGNVTSRRKTAEEKK
QKVRIFLCGDSTGKNEDRKPDGMWGWGSQAYTVFDEAKCTFINCAKAGRSTRTYLLENRW
EEVYRTLRPGDYVLIQFGHNDIGGIDKDKERGVIACAKDTSHVYHLKSNGKNLVVYSFGW
YLRKMIQDCKEKGAIPVLLSFTPRNEWHKGSGTVKGSFYRVKEKKNKQYIERRNDNYIPQ
WCKEIADEQGVAFVDIHNISADFLDKHCGSKEKASLYYNHDHTHTSLLGARNNAASLAKG
LRRINSPLVEYLKK

Enzyme Prediction     

No EC number prediction in MGYG000003515_00315.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE12	364	601	1.5e-50	0.9952380952380953
CE12	65	290	6.8e-47	0.9904761904761905

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd01821	Rhamnogalacturan_acetylesterase_like	1.18e-55	63	290	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.
cd01821	Rhamnogalacturan_acetylesterase_like	1.44e-53	364	601	2	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	3.50e-09	359	608	7	215	Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
cd00229	SGNH_hydrolase	8.70e-08	65	280	1	178	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.
COG2755	TesA	9.85e-05	63	290	9	208	Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADE81450.1	5.77e-201	32	614	17	528
QVJ82319.1	3.63e-197	32	613	17	548
QUT75628.1	7.72e-193	31	613	31	542
BCS85051.1	1.59e-191	2	613	16	553
AND18183.1	2.39e-176	10	613	10	547

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1DEO_A	9.41e-21	365	601	3	212	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	4.34e-20	365	601	3	212	ChainA, Rhamnogalacturonan acetylesterase [Aspergillus aculeatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q00017	7.31e-20	365	601	20	229	Rhamnogalacturonan acetylesterase OS=Aspergillus aculeatus OX=5053 GN=rha1 PE=1 SV=1
Q5BAA2	2.14e-17	365	601	20	224	Rhamnogalacturonan acetylesterase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=AN2528 PE=1 SV=1
O31528	4.57e-14	365	614	5	215	Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
O31523	2.26e-12	360	612	3	223	Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT 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
0.000205	0.999127	0.000158	0.000172	0.000151	0.000138

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003515_00315.