dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Blautia sp900547685

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia sp900547685

CAZyme ID

MGYG000001602_01719

CAZy Family

GH43

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1222	MGYG000001602_35\|CGC1	136733.44	4.1599

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001602	2582611	MAG	China	Asia

Gene Location

Start: 24174; End: 27842 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000001602_01719.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH43	273	565	1.6e-96	0.9715447154471545

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18825	GH43_CtGH43-like	4.89e-138	257	581	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.
cd08985	GH43_CtGH43-like	1.59e-89	257	581	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.
cd18821	GH43_Pc3Gal43A-like	3.55e-87	257	581	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.
NF033930	pneumo_PspA	7.05e-81	1027	1222	444	643	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
NF033930	pneumo_PspA	3.48e-80	1008	1219	444	657	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
AWY99103.1	1	1006	1	1011
QIB57137.1	1	1003	1	1011
QMW81509.1	119	1003	1	882
ALS01207.1	38	926	48	924
AQP53652.1	35	927	39	916

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EUG_A	4.13e-63	245	598	31	374	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]
6EUF_A	2.15e-51	251	612	13	317	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	2.49e-48	246	615	45	360	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]
7BYS_A	3.51e-43	245	584	5	280	ChainA, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYS_B Chain B, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYT_A Chain A, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium]
7BYV_A	8.86e-43	245	584	6	281	ChainA, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium]