CAZyme Information: MGYG000003687_00143

Basic Information

• Species: Paenibacillus polymyxa
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa
• CAZyme ID: MGYG000003687_00143
• CAZy Family: CE7
• CAZyme Description: Cephalosporin-C deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
319	MGYG000003687_1|CGC2	36405.2	5.073

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003687	5656034	Isolate	China	Asia

• Gene Location: Start: 135137; End: 136096 Strand: -

Full Sequence      

MPEDMSLQQLQSYMGSNPKPQDFDIYWERALQELERQSLEYTLEPADFVSPLVECYHLYF
TGVGGARVHGKLARPKHLTEQGPALAMFHGYSCDSGDWFDKVSYAAHGFTVLAMDCRGQG
GLSEDNLQVQGTTVRGHIIRGIDDPDPDRLYYRNVFLDTVQTVRILMSMEQVDPERIGAF
GCSQGGALTVACAALEPRVRVAVPVYPFLSDYKRAWALDATTSAYEELVYYFRWFDPNHV
RESEVFHRLGYIDIQHLADRIRGRVLFVTGLSDVICPPSTQFAVYNKIVSDKELLVYHEY
GHEYLPYLSDRAMSEFLRL

Enzyme Prediction     

EC	3.1.1.72	3.1.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE7	4	318	5.5e-116	0.9904153354632588

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam05448	AXE1	1.77e-141	4	317	4	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	2.11e-124	4	317	5	314	Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
COG1506	DAP2	1.98e-16	12	306	328	598	Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
pfam00326	Peptidase_S9	1.18e-11	105	302	11	187	Prolyl oligopeptidase family.
pfam12146	Hydrolase_4	1.04e-06	84	303	6	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AHM68483.1	5.97e-241	1	319	1	319
AIY09200.1	5.97e-241	1	319	1	319
QPK58024.1	4.03e-239	1	319	1	319
ADO59097.1	4.03e-239	1	319	1	319
AJE51911.1	4.03e-239	1	319	1	319

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FCY_A	4.55e-120	4	319	31	344	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	1.20e-104	11	310	8	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	1.81e-65	4	317	5	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]
1L7A_A	5.71e-60	4	319	5	315	structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis]
2XLB_A	8.52e-60	4	314	5	310	Acetylxylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_B Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_C Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_D Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_E Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_F Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_G Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_H Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_I Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_J Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_K Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_L Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P94388	2.22e-59	4	316	5	312	Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
Q9WXT2	2.03e-43	4	303	5	304	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	1.98e-24	20	296	143	414	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
1.000038	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003687_00143.