dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: HUMAN GUT

help

CAZyme Information: MGYG000002963_04158

You are here: Home > Sequence: MGYG000002963_04158

Basic Information help

Species

Anaerosporobacter mobilis

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerosporobacter; Anaerosporobacter mobilis

CAZyme ID

MGYG000002963_04158

CAZy Family

GH67

CAZyme Description

Xylan alpha-(1->2)-glucuronosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
665	MGYG000002963_46\|CGC1	77057.38	5.6985

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002963	5077023	MAG	United States	North America

Gene Location

Start: 21653; End: 23650 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.139	3.2.1.131

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH67	5	662	1.8e-282	0.9940209267563528

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3661	AguA2	0.0	7	665	11	682	Alpha-glucuronidase [Carbohydrate transport and metabolism].
pfam07488	Glyco_hydro_67M	0.0	114	439	2	324	Glycosyl hydrolase family 67 middle domain. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the central catalytic domain of alpha-glucuronidase.
pfam07477	Glyco_hydro_67C	3.25e-133	441	663	1	223	Glycosyl hydrolase family 67 C-terminus. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the C terminal region of alpha-glucuronidase which is mainly alpha-helical. It wraps around the catalytic domain (pfam07488), making additional interactions both with the N-terminal domain (pfam03648) of its parent monomer and also forming the majority of the dimer-surface with the equivalent C-terminal domain of the other monomer of the dimer.
pfam03648	Glyco_hydro_67N	1.93e-07	6	110	1	120	Glycosyl hydrolase family 67 N-terminus. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the N-terminal region of alpha-glucuronidase. The N-terminal domain forms a two-layer sandwich, each layer being formed by a beta sheet of five strands. A further two helices form part of the interface with the central, catalytic, module (pfam07488).

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCJ94360.1	2.12e-312	1	665	1	658
QHQ61647.1	3.24e-312	1	665	1	660
BCJ97914.1	1.66e-309	1	665	1	668
ABX43513.1	1.87e-305	1	665	18	684
QJU15649.1	2.76e-299	2	665	4	661

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1K9D_A	6.26e-265	3	665	5	678	The1.7 A crystal structure of alpha-D-glucuronidase, a family-67 glycoside hydrolase from Bacillus stearothermophilus T-1 [Geobacillus stearothermophilus],1L8N_A The 1.5A crystal structure of alpha-D-glucuronidase from Bacillus stearothermophilus T-1, complexed with 4-O-methyl-glucuronic acid and xylotriose [Geobacillus stearothermophilus],1MQQ_A THE CRYSTAL STRUCTURE OF ALPHA-D-GLUCURONIDASE FROM BACILLUS STEAROTHERMOPHILUS T-1 COMPLEXED WITH GLUCURONIC ACID [Geobacillus stearothermophilus]
1MQP_A	1.78e-264	3	665	5	678	TheCrystal Structure Of Alpha-D-Glucuronidase From Bacillus Stearothermophilus T-6 [Geobacillus stearothermophilus]
1MQR_A	5.08e-264	3	665	5	678	ChainA, ALPHA-D-GLUCURONIDASE [Geobacillus stearothermophilus]
1K9E_A	1.02e-263	3	665	5	678	ChainA, alpha-D-glucuronidase [Geobacillus stearothermophilus],1K9F_A Chain A, alpha-D-glucuronidase [Geobacillus stearothermophilus]
1GQI_A	1.45e-152	77	655	90	668	Structureof Pseudomonas cellulosa alpha-D-glucuronidase [Cellvibrio japonicus],1GQI_B Structure of Pseudomonas cellulosa alpha-D-glucuronidase [Cellvibrio japonicus],1GQJ_A Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with xylobiose [Cellvibrio japonicus],1GQJ_B Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with xylobiose [Cellvibrio japonicus],1GQK_A Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid [Cellvibrio japonicus],1GQK_B Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid [Cellvibrio japonicus],1GQL_A Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid and xylotriose [Cellvibrio japonicus],1GQL_B Structure of Pseudomonas cellulosa alpha-D-glucuronidase complexed with glucuronic acid and xylotriose [Cellvibrio japonicus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q09LY5	9.77e-264	3	665	5	678	Xylan alpha-(1->2)-glucuronosidase OS=Geobacillus stearothermophilus OX=1422 GN=aguA PE=1 SV=1
P96105	4.43e-251	1	665	1	673	Xylan alpha-(1->2)-glucuronosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=aguA PE=1 SV=2
B8NGU1	1.87e-172	78	662	108	691	Probable alpha-glucuronidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=aguA PE=3 SV=1
B0Y2K1	3.84e-172	82	662	113	692	Probable alpha-glucuronidase A OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=aguA PE=3 SV=1
Q4WW45	3.84e-172	82	662	113	692	Probable alpha-glucuronidase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=aguA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000063	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000002963_04158.