CAZyme Information: MGYG000001346_00799

Basic Information

• Species: Bacteroides uniformis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides uniformis
• CAZyme ID: MGYG000001346_00799
• CAZy Family: GH105
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
719	MGYG000001346_13|CGC4	82462.94	6.6043

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001346	4452540	Isolate	not provided	not provided

• Gene Location: Start: 256937; End: 259096 Strand: +

Full Sequence      

MKTVKFLFVLLFILSTPLQLFGRVTESAENLLRIIHKVNRHWQENNSPQVRSFWDNAAYH
TGNMEVYELTGNTAYLKYSTDWAEYNHWKGAASDNKAEWRYGYGETPQYVLFGDWQCCFQ
TYADLYGIRGDDRRIARAREVLEYQMGTDKNDYWWWADGLYMVMPVMTKLYRITKNPLYL
EKLYEYFSYADSVMYDPEAGLYYRDGSFVYPRHSILGGKKDFWARGDGWVLAAFAKVLQD
LPETDKHRQLYIDRYLAMAGALAKCQHPDGYWTRSLLQHDFAPGPETSGTAFFAYGLQWG
INNGLLDGVVYQPVVDKAWKYLSTVALQPDGSVGYVQPIGGSAIPDQVLSVGSTANFGVG
AFLLAACERYRYLRRESWKDMDGNYINAHGGGILPYNGKYYWFGEHRPAKGFSTQVGITC
YSSDDLANWKYEGVALAVSEEEGSDIERGCIMERPKVIYNGKTGKFVLWFHLELKGRGYG
PARAAVAVSDRPEGPYRFVSSGRVCPGRWPINMTEEEQNATWEDEKYRKWWTPVWHEAIE
KGMFVKRDRQGGQMSRDMTLFTDDDGKAYHIYSSEDNLTLQIAELTEDYLSHSGRYIRIF
PAGHNEAPAIFKKDGTYWMITSGCTGWAPNAARLFSAPSIWGPWTQHPNPCRGEGSDRTF
GGQSTYVLQLPGNRYLFMADIWRPKSLMYSEYLWIPVRFDEEGMPYLTLSGKCNPSDGR

Enzyme Prediction     

No EC number prediction in MGYG000001346_00799.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	395	684	3.8e-98	0.9878048780487805
GH105	45	370	3.7e-78	0.9789156626506024

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18825	GH43_CtGH43-like	1.69e-142	386	699	1	285	Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
pfam07470	Glyco_hydro_88	2.76e-97	33	373	8	343	Glycosyl Hydrolase Family 88. Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases.
cd08985	GH43_CtGH43-like	3.68e-89	386	699	1	273	Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd18822	GH43_CtGH43-like	8.78e-85	386	699	1	266	Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43), Streptomyces avermitilis MA-4680 = NBRC 14893 (Sa1,3Gal43A;SAV2109) (1,3Gal43A), and Ruminiclostridium thermocellum ATCC 27405 (Ct1,3Gal43A;CtGH43;Cthe_0661) (1,3Gal43A). It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd18821	GH43_Pc3Gal43A-like	2.86e-84	386	699	1	262	Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1,3-galactanase (Pc1, 3Gal43A, 1,3Gal43A). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), Fusarium oxysporum 12S Fo/1 (3Gal), and Streptomyces sp. 19(2012) SGalase1 and SGalase2. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRX64606.1	6.08e-315	27	707	38	726
BBK85656.1	1.69e-221	378	719	42	383
QUT33924.1	1.69e-221	378	719	42	383
QUU00374.1	7.85e-220	378	719	42	383
QUT62343.1	4.49e-219	378	719	42	383

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5NOA_A	6.36e-192	23	373	26	375	PolysaccharideLyase BACCELL_00875 [Bacteroides thetaiotaomicron]
6EUG_A	3.69e-189	378	714	35	372	TheGH43, Beta 1,3 Galactosidase, BT3683 with galactoimidazole [Bacteroides thetaiotaomicron],6EUH_A The GH43, Beta 1,3 Galactosidase, BT3683 with galactodeoxynojirimycin [Bacteroides thetaiotaomicron VPI-5482],6EUH_B The GH43, Beta 1,3 Galactosidase, BT3683 with galactodeoxynojirimycin [Bacteroides thetaiotaomicron VPI-5482],6EUH_C The GH43, Beta 1,3 Galactosidase, BT3683 with galactodeoxynojirimycin [Bacteroides thetaiotaomicron VPI-5482],6EUI_A The GH43, Beta 1,3 Galactosidase, BT3683 with galactose [Bacteroides thetaiotaomicron VPI-5482]
4Q88_A	5.35e-169	25	374	10	359	ChainA, Uncharacterized protein [Phocaeicola vulgatus ATCC 8482],4Q88_B Chain B, Uncharacterized protein [Phocaeicola vulgatus ATCC 8482]
6EUF_A	2.92e-57	378	697	11	285	TheGH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUF_B The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUF_C The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUF_D The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUJ_A The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUJ_B The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUJ_C The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUJ_D The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482]
3VSF_A	1.67e-56	378	718	48	351	ChainA, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
L7P9J4	7.21e-48	54	368	60	372	Unsaturated 3S-rhamnoglycuronyl hydrolase OS=Nonlabens ulvanivorans OX=906888 GN=IL45_01505 PE=1 SV=1
T2KPL9	2.42e-46	54	368	58	371	Unsaturated 3S-rhamnoglycuronyl hydrolase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22220 PE=2 SV=1
P9WF04	2.70e-37	154	368	199	407	Unsaturated 3S-rhamnoglycuronyl hydrolase OS=Alteromonas sp. (strain LOR) OX=1537994 GN=LOR_28 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
0.000242	0.999179	0.000164	0.000146	0.000138	0.000130

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001346_00799.