CAZyme Information: MGYG000001518_03418

Basic Information

• Species: Gorillibacterium timonense
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Gorillibacterium; Gorillibacterium timonense
• CAZyme ID: MGYG000001518_03418
• CAZy Family: CE7
• CAZyme Description: Cephalosporin-C deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
320		35865.9	5.5286

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001518	5263339	Isolate	not provided	not provided

• Gene Location: Start: 980188; End: 981150 Strand: +

Full Sequence      

MPLIDMPLDQLKTYPGISPRPDDFDAYWEKALQEMRDTDPALELVPSKFQVPFAECFDLY
FTGVHGARIHAKYVRPRHVQEPHPAVIQFHGYSGHSGDWTDKLGLAALGFSVISMDARGQ
GGKSEDTGGVKGNTLNGHIIRGLDSEDPQHLLFRHIFLDTAQLAGIVMGLPEVDETRVAA
TGWSQGGALTIACAALEPRIWKAAPVYPFLSDYRRVWEMDLAKDAYDELRTYFRLFDPQH
EREESMFHKLGYIDIQNLANRIRAEVLMGIGLMDTICPPSTQMAAYNKIVSTKRLEVFPD
FGHEGLPGLHDKIVGFLLAE

Enzyme Prediction     

EC	3.1.1.72	3.1.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE7	4	313	3.4e-114	0.9744408945686901

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam05448	AXE1	2.78e-161	2	317	1	314	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	1.47e-143	1	317	1	314	Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
COG1506	DAP2	7.67e-16	60	304	369	595	Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
pfam12146	Hydrolase_4	2.35e-10	80	304	1	231	Serine aminopeptidase, S33. This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.
pfam00326	Peptidase_S9	9.82e-09	105	318	10	207	Prolyl oligopeptidase family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASS68552.1	2.14e-184	1	318	1	317
AEI44544.1	1.23e-183	1	317	1	316
AFH64655.1	2.49e-183	1	317	1	316
AFC32345.1	3.54e-183	1	317	1	316
AJY75725.1	1.22e-181	1	319	1	318

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FCY_A	7.53e-153	1	318	27	342	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	4.14e-90	8	311	4	306	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	1.06e-67	1	319	1	319	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]
1L7A_A	7.25e-58	1	316	1	311	structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis]
1ODS_A	2.03e-57	1	316	1	311	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P94388	7.89e-57	1	316	1	311	Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
Q9WXT2	3.05e-47	1	305	1	305	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	3.60e-21	11	299	136	416	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
1.000072	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001518_03418.