CAZyme Information: MGYG000000069_02761

Basic Information

• Species: Clostridium_A leptum
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Clostridium_A; Clostridium_A leptum
• CAZyme ID: MGYG000000069_02761
• CAZy Family: CBM35
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1710	MGYG000000069_21|CGC1	186399.88	4.1481

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000069	3099132	Isolate	United Kingdom	Europe

• Gene Location: Start: 2394; End: 7526 Strand: -

Full Sequence      

MEYITRGCFFVFCNLLLYEIGAQMKGEKKVGQFKKIVRGITAGLMSAAVLMSGMVANASL
QANAAGLEATPPEGAPETAVLVEAETGEFKWEWRSGTNDDHPCSGTFVSIGGDIEDARAQ
WEVEVETAGTYQFAFSYVAGAVGGWPDDRSIRLLVNGTEQAIETFTGTGNWDDWIYHSVE
LNLEAGENVVTVQTNGKNNGVNIDYFYYWLLEAAEPMPELIPPNATHMEAEDADVGGGAR
GGDRSHSGYSGDSFVSGFENHKGAYVEFTYNAEEAGEYYLSLRYANGHNNGWPDTKQIGL
SVNDGEITMVPFTVTAAWNQWEENVVKVTLEKGENKIRYQNVDGEREGVVNIDKIAIWPH
VADPTVDTLVFENTSYSLRVGATVKPMVYAIDSNGLKMPYDGEITFRFEDEESASYNKED
GTIKALKAGEYKVYAEGPGIKTPGEATLKIVANPTISVDFSSVERPVNHSQFGYILIPNY
NIPDSRLTLLGPLLARDTIPAQNFQGVGDMGGYYDYEYSILQRSLQAVQRAKDAGHKYYF
LLGHNPSWATASGNPTDTGLVKDEEELARFKQYLKDTLQYYKDNGITPDFANLTNEYWTG
LFPTYQVAWEAVREVYPDFIPAVGPSAVGFDGIPEFYIPESVEAGITVEGPAWHEFWTGD
TFISYDKLKDHVDYIADLQEQYPEANGKYIIFEENNSGGVNAGGPSGTAIDFTRTMSNII
RTNIDWNIKGCLEGGNANGMSDIITANKEKVTQNPAVRRPLWWVYYAFSKMSGDYVTVSV
DAPNDKNGEFTGAASKDVDDSKVIIANSSTDGSVSVELNNQPYVGEDVQVDLYKVITSDL
EGLDYPGENDGLMYQRTLDVESTENISVVIDGVKANETWMVVLKKVESAPSFFHPMTPDD
GEAAVTTPTLTWSKAQGATSYTVAVSANKDMSDPIIEESGIEGQSFEVPEKAGLKLGQRY
YWTVSAENEYGSTELPERVVYSFYTSESTEVPGQFSPTMPSLGAMNEKTRPEFKWTTAYQ
ADSYRLVVSKNEDLSDPVINESGITNVRGNGQFGGNSQAYYTPTRDQEFEYETTYYWTVY
AVNDEGERPWNGPIHSFTTKAEGDAPKDFKLTSPADQAEEVSARTALTWEASANAFFYKL
EISENEDMSDPVLVRDRMIYNKYTMEPNVLKPDTTYYWRVTALTKDLKHETASSTGIRSF
KTEAVPCSPLLYAEYAEGSTVNLLFQESIGATSYTIKYGTEPGSYTKEITNVTGTPCQIE
DMEEGTYYFAVVANNAEGSSDIWNERSVTVGGEAEVTPVLDEIAIEGPAKLKYKVGESLD
TTGLVVTAKYSDGTEKVLAAEDYDVEGFDSSTAGEKTVTVVYEEGGVAKTAEFEITVIEA
VGITVTKLPNKTEYFVGEKLDQTGIQVSLKYSDNSTEPLAAGYSLAQYDPDKVGKQQIRV
QYMNFVAYFEVTVKERPAHLALESISVKAPDKTEYFVGDKLDETGMVVTATYSDGSSRAV
SGYEVDFDSSKAGKATVTVSYTEDGVTKTAAFEVTVKEKPVEVTLESITVTAPTKTEYAI
GDELDLAGVVVTAKYSDGTEKVLAAEDYVVSAFDSSTAGEKQVTVSYTEGGVTKTAAFTV
TVKESSGSSEDPGTSEDPGSSEDPGSSEGPGTGSSGSESGGTESGTGSGTENNNNAQTGD
GMTVPIILLSLLVAASAGIAVVLGKKRRLG

Enzyme Prediction     

No EC number prediction in MGYG000000069_02761.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM35	229	356	8.7e-26	0.9747899159663865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04083	CBM35_Lmo2446-like	1.06e-26	226	357	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.
cd04082	CBM35_pectate_lyase-like	2.70e-23	229	357	4	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.
cd04082	CBM35_pectate_lyase-like	1.08e-15	110	207	34	123	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.
cd04081	CBM35_galactosidase-like	1.70e-15	229	357	4	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.
cd04083	CBM35_Lmo2446-like	2.19e-15	83	206	4	123	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANY70025.1	0.0	64	1376	29	1402
BAM48288.1	0.0	217	1289	6	1057
AGI38277.1	2.80e-36	1310	1606	239	537
AGC67199.1	2.80e-36	1310	1606	239	537
ANW97669.1	2.80e-36	1310	1606	239	537

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5X7O_A	1.94e-19	94	357	851	1097	Crystalstructure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase [Paenibacillus sp. 598K],5X7O_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase [Paenibacillus sp. 598K],5X7P_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with acarbose [Paenibacillus sp. 598K],5X7P_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with acarbose [Paenibacillus sp. 598K],5X7Q_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with maltohexaose [Paenibacillus sp. 598K],5X7Q_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with maltohexaose [Paenibacillus sp. 598K],5X7R_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with isomaltohexaose [Paenibacillus sp. 598K],5X7R_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase complexed with isomaltohexaose [Paenibacillus sp. 598K],5X7S_A Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase, terbium derivative [Paenibacillus sp. 598K],5X7S_B Crystal structure of Paenibacillus sp. 598K alpha-1,6-glucosyltransferase, terbium derivative [Paenibacillus sp. 598K]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0A401ETL2	1.27e-13	1463	1626	1296	1455	Exo-beta-1,6-galactobiohydrolase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=bl1,6Gal 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
0.500247	0.362904	0.121231	0.013970	0.001389	0.000257

TMHMM  Annotations     

start	end
1682	1704