dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001512_03203

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Basic Information help

Species

Coprobacter secundus

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Coprobacteraceae; Coprobacter; Coprobacter secundus

CAZyme ID

MGYG000001512_03203

CAZy Family

CE7

CAZyme Description

Acetyl esterase Axe7A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
430	MGYG000001512_19\|CGC33	48359.6	8.4792

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001512	4253015	Isolate	not provided	not provided

Gene Location

Start: 1530729; End: 1532021 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001512_03203.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
CE7	122	417	5.9e-86	0.9424920127795527

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3458	Axe1	1.73e-50	120	413	10	303	Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
pfam05448	AXE1	2.49e-47	120	409	9	299	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	2.70e-13	163	427	358	617	Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
COG0412	DLH	2.45e-06	173	385	6	174	Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism].
pfam00326	Peptidase_S9	8.70e-05	278	429	57	212	Prolyl oligopeptidase family.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCI64863.1	0.0	1	430	1	430
SCM59450.1	5.86e-172	24	425	31	430
BBD44595.1	4.77e-171	2	424	13	429
QNF34741.1	2.60e-162	6	430	15	440
QGY47410.1	1.45e-161	6	426	10	423

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6AGQ_A	2.00e-33	125	423	15	317	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	4.51e-30	119	409	14	298	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]
1L7A_A	4.51e-30	119	409	14	298	structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis]
1ODT_C	1.19e-29	119	409	14	298	cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [Bacillus subtilis]
5HFN_A	7.14e-29	120	409	22	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	7.60e-102	29	426	45	437	Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1
P94388	1.79e-29	119	409	14	298	Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
Q9WXT2	5.09e-28	120	409	10	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 OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.709384	0.269638	0.018307	0.000715	0.000598	0.001352

TMHMM Annotations help

There is no transmembrane helices in MGYG000001512_03203.