dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002414_01902

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Basic Information help

Species

Paenibacillus odorifer

Lineage

Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus odorifer

CAZyme ID

MGYG000002414_01902

CAZy Family

CBM9

CAZyme Description

Acetyl esterase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
693	MGYG000002414_1\|CGC41	76734.25	4.5972

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002414	6802552	Isolate	South Korea	Asia

Gene Location

Start: 2198838; End: 2200919 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002414_01902.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CBM9	502	690	3.8e-24	0.9835164835164835

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	2.50e-61	502	692	1	188	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates.
COG0657	Aes	1.00e-33	90	281	62	288	Acetyl esterase/lipase [Lipid transport and metabolism].
cd09619	CBM9_like_4	1.59e-20	498	688	1	181	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other domains.
pfam07859	Abhydrolase_3	1.50e-19	110	281	1	207	alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.
COG1506	DAP2	1.59e-18	96	297	382	613	Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWV32829.1	0.0	1	693	1	693
AIQ23053.1	0.0	1	692	1	693
AIQ34891.1	0.0	1	692	1	693
BBI33533.1	8.52e-278	1	692	1	694
QJD85603.1	4.86e-154	1	692	1	692

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5AO9_A	3.73e-15	92	283	28	252	Thestructure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-native [Thermogutta terrifontis],5AOA_A The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-Propionate bound [Thermogutta terrifontis],5AOB_A The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-butyrate bound [Thermogutta terrifontis],5AOC_A The structure of a novel thermophilic esterase from the Planctomycetes species, Thermogutta terrifontis, Est2-valerate bound [Thermogutta terrifontis]
7BFN_A	3.78e-15	92	283	29	253	ChainA, Esterase [Thermogutta terrifontis]
7BFO_A	1.67e-14	92	283	29	253	ChainA, Esterase [Thermogutta terrifontis],7BFR_A Chain A, Esterase [Thermogutta terrifontis],7BFT_A Chain A, Esterase [Thermogutta terrifontis],7BFU_A Chain A, Esterase [Thermogutta terrifontis],7BFV_A Chain A, Esterase [Thermogutta terrifontis]
1QZ3_A	3.30e-12	92	210	60	170	CRYSTALSTRUCTURE OF MUTANT M211S/R215L OF CARBOXYLESTERASE EST2 COMPLEXED WITH HEXADECANESULFONATE [Alicyclobacillus acidocaldarius],1U4N_A Crystal Structure Analysis of the M211S/R215L EST2 mutant [Alicyclobacillus acidocaldarius]
4N5H_X	4.73e-12	73	199	31	152	ChainX, Esterase/lipase [Lacticaseibacillus rhamnosus Lc 705],4N5I_X Chain X, Esterase/lipase [Lacticaseibacillus rhamnosus Lc 705],4OUK_X Chain X, Esterase B [Lacticaseibacillus rhamnosus HN001],4PO3_X Chain X, Esterase B [Lacticaseibacillus rhamnosus HN001]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q6L5F5	3.84e-12	93	279	130	355	Probable isoprenylcysteine alpha-carbonyl methylesterase ICME OS=Oryza sativa subsp. japonica OX=39947 GN=IMCE PE=2 SV=1
Q5Z9I2	1.60e-10	88	279	133	366	Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL1 OS=Oryza sativa subsp. japonica OX=39947 GN=IMCEL1 PE=2 SV=1
Q8VYP9	2.34e-09	73	279	180	420	Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL1 OS=Arabidopsis thaliana OX=3702 GN=ICMEL1 PE=2 SV=1
P96402	7.67e-09	79	281	127	369	Esterase LipC OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=lipC PE=1 SV=1
W7MTJ1	1.16e-08	91	281	59	287	Esterase FVEG_12639 OS=Gibberella moniliformis (strain M3125 / FGSC 7600) OX=334819 GN=FVEG_12639 PE=2 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
0.811084	0.147060	0.039353	0.000486	0.000318	0.001706

TMHMM Annotations download full data without filtering help

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