dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000222_03394

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Basic Information help

Species

Parabacteroides sp003473295

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp003473295

CAZyme ID

MGYG000000222_03394

CAZy Family

CE7

CAZyme Description

Acetyl esterase Axe7A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
425	MGYG000000222_44\|CGC1	48157.81	7.9376

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000222	4189286	Isolate	China	Asia

Gene Location

Start: 14987; End: 16264 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000222_03394.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CE7	127	420	7.8e-90	0.9648562300319489

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3458	Axe1	2.17e-52	119	421	1	315	Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
pfam05448	AXE1	1.88e-50	136	421	20	315	Acetyl xylan esterase (AXE1). This family consists of several bacterial acetyl xylan esterase proteins. Acetyl xylan esterases are enzymes that hydrolyze the ester linkages of the acetyl groups in position 2 and/or 3 of the xylose moieties of natural acetylated xylan from hardwood. These enzymes are one of the accessory enzymes which are part of the xylanolytic system, together with xylanases, beta-xylosidases, alpha-arabinofuranosidases and methylglucuronidases; these are all required for the complete hydrolysis of xylan.
COG1506	DAP2	2.40e-06	183	417	375	605	Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
COG0412	DLH	2.74e-05	182	322	10	146	Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT49362.1	3.09e-251	1	420	1	420
QRM99790.1	1.20e-232	1	420	1	420
QUT31430.1	1.20e-232	1	420	1	420
BCG54171.1	1.39e-213	1	422	3	425
QUT54228.1	9.16e-171	1	421	1	423

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6AGQ_A	3.60e-38	119	406	1	303	Acetylxylan esterase from Paenibacillus sp. R4 [Paenibacillus sp. R4],6AGQ_B Acetyl xylan esterase from Paenibacillus sp. R4 [Paenibacillus sp. R4],6AGQ_C Acetyl xylan esterase from Paenibacillus sp. R4 [Paenibacillus sp. R4],6AGQ_D Acetyl xylan esterase from Paenibacillus sp. R4 [Paenibacillus sp. R4],6AGQ_E Acetyl xylan esterase from Paenibacillus sp. R4 [Paenibacillus sp. R4],6AGQ_F Acetyl xylan esterase from Paenibacillus sp. R4 [Paenibacillus sp. R4]
1ODS_A	1.10e-29	130	425	15	317	CephalosporinC deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_B Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_C Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_D Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_E Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_F Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_G Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_H Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis]
1ODT_C	2.90e-29	130	425	15	317	cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [Bacillus subtilis]
1L7A_A	2.90e-29	130	422	15	314	structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis]
5HFN_A	4.82e-29	130	406	27	289	Crystalstructure of a loop truncation variant of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 2.75 Angstrom resolution [Thermotoga maritima MSB8],5HFN_B Crystal structure of a loop truncation variant of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 2.75 Angstrom resolution [Thermotoga maritima MSB8],5HFN_C Crystal structure of a loop truncation variant of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 2.75 Angstrom resolution [Thermotoga maritima MSB8],5HFN_D Crystal structure of a loop truncation variant of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 2.75 Angstrom resolution [Thermotoga maritima MSB8],5HFN_E Crystal structure of a loop truncation variant of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 2.75 Angstrom resolution [Thermotoga maritima MSB8],5HFN_F Crystal structure of a loop truncation variant of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 2.75 Angstrom resolution [Thermotoga maritima MSB8]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
D5EXI2	1.14e-90	1	425	12	439	Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1
P94388	6.04e-29	130	425	15	317	Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
Q9WXT2	1.71e-27	130	406	15	303	Cephalosporin-C deacetylase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=axeA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000928	0.997946	0.000428	0.000247	0.000207	0.000197

TMHMM Annotations help

There is no transmembrane helices in MGYG000000222_03394.