CAZyme Information: MGYG000004157_02123

Basic Information

• Species: HGM11514 sp900757255
• Lineage: Bacteria; Firmicutes_A; Clostridia; HGM11514; HGM11514; HGM11514; HGM11514 sp900757255
• CAZyme ID: MGYG000004157_02123
• CAZy Family: CE7
• CAZyme Description: Cephalosporin-C deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
316		35690.71	5.4076

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004157	2480742	MAG	United Kingdom	Europe

• Gene Location: Start: 3229; End: 4179 Strand: -

Full Sequence      

MGIDMPIEQLQNYQGQNPKPADWEKYWERALHELDQTDPQPELIKSDFKVPNAECFDLYF
NGVKSCRIHAKLIKPSNIEKKAPAMLMFHGYSDSAGEWNQKLNYTSIGFVVAAMDVRGQG
GLSEDLNPVRGTTLNGHIVRGIDDPDPDNLFFRQVFLDTAQLARVLMSFDFVDENRLAVK
GGSQGGALTLACAALVPQIKKIAVWYPFLSDFKRSYEMGHAPAEIPTYFRKCNPDHSREE
EVFQKLGYIDVQFLAPKIKAEVLFFTGLTDVTCPPSTQAAVYNKLTCKKKQLFYPDFGHE
DLTGSNDIAMQFFLDL

Enzyme Prediction     

No EC number prediction in MGYG000004157_02123.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE7	3	313	4.9e-104	0.987220447284345

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam05448	AXE1	2.97e-132	3	314	3	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	7.67e-117	3	316	4	317	Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
COG1506	DAP2	1.05e-13	60	315	373	615	Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
pfam00326	Peptidase_S9	2.05e-11	98	308	5	196	Prolyl oligopeptidase family.
pfam12146	Hydrolase_4	3.22e-05	84	300	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
QKS47765.1	7.66e-137	3	315	4	318
ANY71421.1	3.59e-135	3	314	4	317
AGC68434.1	7.49e-135	3	316	4	320
AGI39454.1	7.49e-135	3	316	4	320
ANW98805.1	7.49e-135	3	316	4	320

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FCY_A	2.31e-124	1	316	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	1.22e-85	7	307	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	2.24e-59	3	312	4	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]
1ODS_A	4.12e-52	3	313	4	312	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	4.12e-52	3	313	4	312	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	1.14e-51	3	313	4	312	Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
Q9WXT2	4.14e-46	3	300	4	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	2.49e-19	20	310	143	431	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
1.000084	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004157_02123.