CAZyme Information: MGYG000002881_00744

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus
• CAZyme ID: MGYG000002881_00744
• CAZy Family: CBM35
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
394		43056.59	4.3845

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002881	1270591	MAG	United States	North America

• Gene Location: Start: 70; End: 1254 Strand: +

Full Sequence      

MTTAEPTAPQTTAKVTTTDPRYFAADQTLNNGVTETVNAGYTREDGYVNLANELDSSITF
NVNVAIDGNYMTHIRFANGSADDRKMKVYVNGNTADYWMQSFTGTGAWTEWKEFGIVLPL
KSGNNTIQFVSATAEGGPNLDYITLALTDEPYAETYDPAQDLPPVGSDKPTVYIAGDSTV
QSYRESYAPQQGWGYYLQSKFDDDVTVVNNSIAGRSTKKFYDEGRWQSIVDNLKDGDFVM
IQFAINDSGASNEDRYAPTCGDVDNPSAGSYEWYMTEFIKTAKEKGATPILVTTVIGMKA
YSGGKFVNSYSNYCDACKKLAAKYSVPCIDLNTLMVDHYNSVGYDTAKSYHLMGAVEGST
DGTHFCEKGAEIVAGLVANAVKTQNITGLENHVK

Enzyme Prediction     

EC	3.1.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE12	171	380	1.3e-64	0.9904761904761905
CBM35	22	145	5.6e-23	0.9915966386554622

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd01821	Rhamnogalacturan_acetylesterase_like	9.49e-70	170	378	1	195	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.
cd04082	CBM35_pectate_lyase-like	4.81e-49	21	145	2	124	Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. This family includes carbohydrate binding module family 35 (CBM35) domains that are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. Included in this family are CBM35s of pectate lyases, including pectate lyase 10A from Cellvibrio japonicas, these enzymes release delta-4,5-anhydrogalaturonic acid (delta4,5-GalA) from pectin, thus identifying a signature molecule for plant cell wall degradation. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. Some CBM35s bind their ligands in a calcium-dependent manner, especially those binding uronic acids.
cd04083	CBM35_Lmo2446-like	1.23e-19	20	145	1	125	Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446. This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes. Some CBM35 domains belonging to this family are appended to glycoside hydrolase (GH) family domains, including glycoside hydrolase family 31 (GH31), for example the CBM35 domain of Lmo2446, an uncharacterized protein from Listeria monocytogenes EGD-e. These CBM35s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. GH31 has a wide range of hydrolytic activities such as alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, or alpha-1,4-glucan lyase, cleaving a terminal carbohydrate moiety from a substrate that may be a starch or a glycoprotein. Most characterized GH31 enzymes are alpha-glucosidases.
cd04081	CBM35_galactosidase-like	1.97e-14	22	145	3	125	Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. This family includes carbohydrate binding module family 35 (CBM35); these are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. Examples of proteins which contain CBM35s belonging to this family includes the CBM35 of an exo-beta-1,3-galactanase from Phanerochaete chrysosporium 9 (Pc1,3Gal43A) which is appended to a GH43 domain, and the CBM35 domain of two bifunctional proteins with beta-L-arabinopyranosidase/alpha-D-galactopyranosidase activities from Fusarium oxysporum 12S, Foap1 and Foap2 (Fo/AP1 and Fo/AP2), that are appended to GH27 domains. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). Some CBM35s bind their ligands in a calcium-dependent manner. In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates, while family GH27 includes alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases.
COG2755	TesA	2.07e-14	170	389	9	216	Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL17979.1	3.33e-154	21	394	626	996
ADU21040.1	1.80e-141	19	394	639	1020
ANV75445.1	9.60e-82	22	386	482	822
ALX07703.1	9.60e-82	22	386	482	822
ABN54336.1	9.60e-82	22	386	482	822

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2W47_A	1.98e-26	22	143	7	126	ChainA, Lipolytic Enzyme, G-d-s-l [Acetivibrio thermocellus]
2W1W_A	2.10e-26	22	143	7	126	ChainA, LIPOLYTIC ENZYME, G-D-S-L [Acetivibrio thermocellus],2W1W_B Chain B, LIPOLYTIC ENZYME, G-D-S-L [Acetivibrio thermocellus]
1DEO_A	3.70e-20	171	381	2	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	1.80e-19	171	381	2	212	ChainA, Rhamnogalacturonan acetylesterase [Aspergillus aculeatus]
2VZP_A	1.26e-17	22	145	6	127	AtomicResolution Structure of the C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA [Amycolatopsis orientalis],2VZP_B Atomic Resolution Structure of the C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA [Amycolatopsis orientalis],2VZQ_A C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA in complex with digalacturonic acid [Amycolatopsis orientalis],2VZQ_B C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA in complex with digalacturonic acid [Amycolatopsis orientalis],2VZR_A C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA in complex with glucuronic acid [Amycolatopsis orientalis],2VZR_B C-terminal CBM35 from Amycolatopsis orientalis exo-chitosanase CsxA in complex with glucuronic acid [Amycolatopsis orientalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31528	1.05e-38	172	394	5	215	Probable rhamnogalacturonan acetylesterase YesY OS=Bacillus subtilis (strain 168) OX=224308 GN=yesY PE=1 SV=1
O31523	1.48e-30	172	393	8	223	Rhamnogalacturonan acetylesterase RhgT OS=Bacillus subtilis (strain 168) OX=224308 GN=rhgT PE=1 SV=1
Q00017	2.80e-19	171	381	19	229	Rhamnogalacturonan acetylesterase OS=Aspergillus aculeatus OX=5053 GN=rha1 PE=1 SV=1
Q5BAA2	3.87e-17	171	381	19	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
Q56F26	1.00e-14	22	145	911	1032	Exo-beta-D-glucosaminidase OS=Amycolatopsis orientalis OX=31958 GN=csxA PE=1 SV=2

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
0.991468	0.008519	0.000025	0.000011	0.000007	0.000013

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002881_00744.