CAZyme Information: MGYG000000785_00134

Basic Information

• Species: Lancefieldella sp900555335
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Atopobiaceae; Lancefieldella; Lancefieldella sp900555335
• CAZyme ID: MGYG000000785_00134
• CAZy Family: CE7
• CAZyme Description: Cephalosporin-C deacetylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
346	MGYG000000785_4|CGC1	38087.7	4.2532

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000785	1185697	MAG	China	Asia

• Gene Location: Start: 13433; End: 14473 Strand: +

Full Sequence      

MHQETLELAELKAAHALTPYPSDFEAFWKARMEEADNAPLSWQIVPSTEVTSTASAHFFD
LTFVGIDGAEIYAKYLRPQTASGVQTPLVLQFHGYPGSSRSWFEQSSFLGLGCSLIALDN
PGQGGRSLDGSSYKSTTVSGHLVLGLDGPVEDLYFVHLYQNIRLLCRIVRQLEGIDTDRV
FVNGASQGGGIGLATCALNQDLINRAAILYPFLTDFRCVWELNADEVAYEGIRYYSRWFD
ADGSRVDEVFAKLAYIDSANFARLVTCPVLFGTGLDDPVVPPEAQFAAYNALTCPKRHLL
YPGYAHEEIGDFDDKIIDFFCSENGEQALEVLDSSFPAQAEGEVCA

Enzyme Prediction     

No EC number prediction in MGYG000000785_00134.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE7	5	320	1.7e-90	0.987220447284345

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3458	Axe1	2.07e-80	6	321	6	315	Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
pfam05448	AXE1	7.88e-80	6	321	5	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.
COG1506	DAP2	1.52e-12	62	320	369	613	Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
COG0596	MhpC	4.92e-08	62	320	3	279	Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only].
COG2267	PldB	2.60e-05	60	320	11	291	Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACV51360.1	1.12e-245	1	346	1	346
ANU40725.1	2.17e-145	18	326	18	323
QQR06497.1	2.17e-145	18	326	18	323
SDR65558.1	3.18e-140	7	320	6	320
AZH69971.1	3.29e-140	19	321	19	318

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3FCY_A	1.76e-67	6	319	32	340	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	6.99e-54	21	314	17	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	2.67e-36	22	319	22	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	3.87e-29	6	312	18	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]
3M81_A	1.97e-28	6	312	18	321	Crystalstructure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_B Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_C Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_D Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_E Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_F Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],5FDF_A Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_B Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_C Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_D Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_E Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_F Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5JIB_A Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_B Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_C Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_D Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_E Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_F Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9WXT2	8.76e-28	6	312	6	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
P94388	1.87e-24	6	320	6	312	Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
D5EXI2	1.40e-20	17	306	136	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
1.000072	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000785_00134.