CAZyme Information: MGYG000000047_00470

Basic Information

• Species: Clostridium disporicum_A
• Lineage: Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium disporicum_A
• CAZyme ID: MGYG000000047_00470
• CAZy Family: CE7
• CAZyme Description: Cephalosporin-C deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
321	MGYG000000047_2|CGC2	36537.77	4.6222

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000047	3448648	Isolate	United Kingdom	Europe

• Gene Location: Start: 236735; End: 237700 Strand: +

Full Sequence      

MPIVDMPLERLREYKGTNTLPSDFSEFWNERINEVKNHPLKYKITESEIRGFEGCEFLDL
WFKGIDGGKVYAKYIRPKTDEDVPLILQFHGYPGASRGWFEQLSFVGMGCAIIAMDCPGQ
GGNGDSYTNMKGTTVSGHIVAGLDGDICNMYYVKLFQNASILCRIVKELNGIDKERIYAN
GASQGAGIALVCAALNPIIKKCAALYPFLSDYKRVWDMDLDMIAYEGLRYYSRWFNPMND
KEDEMFTKLGYIDVHNFADMINCEVLFGTGLMDNVCPPSTQFAIYNNIGSKKKHIIFPDY
THEEIGEFDDMLIDFFLKEDD

Enzyme Prediction     

No EC number prediction in MGYG000000047_00470.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE7	4	315	6.1e-98	0.987220447284345

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam05448	AXE1	1.30e-104	2	318	1	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.
COG3458	Axe1	6.30e-95	1	318	1	315	Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
COG1506	DAP2	8.86e-16	61	303	369	595	Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
pfam00326	Peptidase_S9	0.001	172	318	61	208	Prolyl oligopeptidase family.
COG0400	YpfH	0.010	155	206	76	130	Predicted esterase [General function prediction only].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSX02335.1	1.82e-195	1	321	1	321
QCJ05782.1	1.82e-195	1	321	1	321
QJU43156.1	1.82e-195	1	321	1	321
AXB83863.1	1.82e-195	1	321	1	321
QGH23486.1	2.59e-195	1	321	1	321

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FCY_A	1.38e-104	1	318	27	343	CrystalStructure of Acetyl Xylan Esterase 1 from Thermoanaerobacterium sp. JW/SL YS485 [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3FCY_B Crystal Structure of Acetyl Xylan Esterase 1 from Thermoanaerobacterium sp. JW/SL YS485 [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3FCY_C Crystal Structure of Acetyl Xylan Esterase 1 from Thermoanaerobacterium sp. JW/SL YS485 [Thermoanaerobacterium saccharolyticum JW/SL-YS485]
7CUZ_A	1.51e-82	12	312	8	308	ChainA, Acetylxylan esterase [Lactococcus lactis subsp. lactis KF147],7CUZ_B Chain B, Acetylxylan esterase [Lactococcus lactis subsp. lactis KF147],7CUZ_C Chain C, Acetylxylan esterase [Lactococcus lactis subsp. lactis KF147],7CUZ_D Chain D, Acetylxylan esterase [Lactococcus lactis subsp. lactis KF147]
6AGQ_A	9.17e-45	1	315	1	316	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]
5GMA_A	3.72e-44	1	308	13	321	Crystalstructure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_B Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_C Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_D Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_E Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_F Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8]
1L7A_A	9.15e-44	1	318	1	314	structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P94388	2.54e-43	1	318	1	314	Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
Q9WXT2	8.32e-43	1	308	1	309	Cephalosporin-C deacetylase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=axeA PE=1 SV=1
D5EXI2	1.26e-20	21	307	143	425	Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000050	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000047_00470.