CAZyme Information: MGYG000000403_00337

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA1381; UBA4716
• CAZyme ID: MGYG000000403_00337
• CAZy Family: CE7
• CAZyme Description: Cephalosporin-C deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
321	MGYG000000403_52|CGC1	36696.15	5.638

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000403	2138464	MAG	Sweden	Europe

• Gene Location: Start: 1343; End: 2308 Strand: -

Full Sequence      

MPLIDMPLEKLKKYMGTNPRPDDFDEYWERGLKEMGETNPETQLVKNKFQLPYADCFDLY
FNGTKNGRIHAKLLIPKNIKGKAPVLLHFHGYYGKSHNWMYYAGFAAMGFIVAGMDCRGQ
AGLSDDKNPVCGNNISGHIIRGLDEPNPDNMYYRNVFLDTAMLARVVSELEQADGDKMAA
FGGSQGGALTVACACLVPNLKMAAPCYPFLSDYKRVWDMDLDQRAYDEIRSYFRMFDPCH
ERENEIFTKLGYIDLHNMAERINAKMMFGTGLMDDVCPPSTQFAVYNRIKSEKSMVIYPD
FGHENLPDFEEKMTEMFCKLL

Enzyme Prediction     

EC	3.1.1.72	3.1.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE7	4	314	3.2e-108	0.9776357827476039

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam05448	AXE1	1.51e-138	2	311	1	307	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	8.61e-123	1	311	1	307	Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
COG1506	DAP2	1.15e-11	68	304	377	595	Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
pfam00326	Peptidase_S9	4.59e-09	105	321	10	210	Prolyl oligopeptidase family.
pfam12146	Hydrolase_4	4.02e-06	85	304	8	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
AGC68434.1	6.53e-142	1	311	1	311
AGI39454.1	6.53e-142	1	311	1	311
ANW98805.1	6.53e-142	1	311	1	311
ANX01307.1	6.53e-142	1	311	1	311
BCK00061.1	6.30e-137	1	317	1	316

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FCY_A	5.24e-122	1	320	27	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	1.38e-80	14	315	10	310	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	6.36e-57	1	313	1	313	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	6.72e-52	1	321	1	316	structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis]
2XLB_A	1.40e-51	1	321	1	316	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	1.03e-50	1	317	1	312	Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
Q9WXT2	6.70e-46	1	321	1	321	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	2.69e-21	9	303	134	420	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
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000403_00337.