dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000135_01803

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Basic Information help

Species

Murimonas intestini

Lineage

Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Murimonas; Murimonas intestini

CAZyme ID

MGYG000000135_01803

CAZy Family

GH67

CAZyme Description

Xylan alpha-(1->2)-glucuronosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
660	MGYG000000135_3\|CGC11	74868.47	5.2795

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000135	5745007	Isolate	Canada	North America

Gene Location

Start: 332738; End: 334720 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	657	1.7e-280	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	660	11	682	Alpha-glucuronidase [Carbohydrate transport and metabolism].
pfam07488	Glyco_hydro_67M	0.0	108	434	1	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	3.77e-140	436	657	1	222	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	4.56e-08	6	105	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).
pfam02838	Glyco_hydro_20b	9.23e-07	37	101	36	100	Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QJU15649.1	0.0	3	660	5	661
QQQ91839.1	0.0	3	660	5	661
ANU78479.1	0.0	3	660	12	668
ASU31294.1	0.0	3	660	5	661
BCJ97914.1	7.58e-318	1	660	1	668

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1K9D_A	3.96e-262	3	660	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	7.95e-262	3	660	5	678	TheCrystal Structure Of Alpha-D-Glucuronidase From Bacillus Stearothermophilus T-6 [Geobacillus stearothermophilus]
1MQR_A	2.27e-261	3	660	5	678	ChainA, ALPHA-D-GLUCURONIDASE [Geobacillus stearothermophilus]
1K9E_A	4.56e-261	3	660	5	678	ChainA, alpha-D-glucuronidase [Geobacillus stearothermophilus],1K9F_A Chain A, alpha-D-glucuronidase [Geobacillus stearothermophilus]
1GQI_A	3.22e-143	73	645	91	663	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	4.35e-261	3	660	5	678	Xylan alpha-(1->2)-glucuronosidase OS=Geobacillus stearothermophilus OX=1422 GN=aguA PE=1 SV=1
P96105	9.80e-244	71	660	80	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
Q5AQZ4	7.93e-172	60	657	98	699	Alpha-glucuronidase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=aguA PE=1 SV=1
B8NGU1	1.25e-171	5	657	23	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
A1CC12	4.05e-170	72	657	108	692	Probable alpha-glucuronidase A OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 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
1.000053	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000135_01803.