CAZyme Information: MGYG000002027_00474

Basic Information

• Species: HGM11377 sp900755035
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-917; HGM11377; HGM11377 sp900755035
• CAZyme ID: MGYG000002027_00474
• CAZy Family: GH2
• CAZyme Description: Beta-galactosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
840		97937.18	6.8315

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002027	1634201	MAG	Spain	Europe

• Gene Location: Start: 19303; End: 21825 Strand: -

Full Sequence      

MRKYLHDNWQLYNTKHDKIRATVPGCNYLDLMDNGVIKDPFLKTNEKDTLWVANEDWIYE
TSFNMTSSELDFDSLTINFKQLDTICDVFLNGRPILKANNCFLPYQVDVKRVLVNGENKL
SVYFYSPVNYVKEKQSKVKCPRNSNGLTGIPHIRKPGYHFGWDWGPNLPLSGITDSVYIE
GHNYAKLDDVLIAQSHHDSVDVKVDVKVKKFRNVKSVVKVELTYPSGETHEKTTNDNGEV
TFTVDNPILWQPNGYTDRKTQPLYKITTSLIVNGKVIDENVKNVGLRTIELDRSKDEYGS
NFCFKVNGNPIFMKGANYIPTDSFITRQYGDLEKYVKVAVDSNFNMLRIWGGGYYGSSEL
YDLCDKYGILLWQDFAFACQPYPFFNDEFTQNVLDEVEANVKRLRHHACLALWCGNNEIE
VMSPAWLNRKEFVKWTEKFFYDILPNKLRKFDGVTPYIPGTPVGYSHNKGVSDDNVGDTH
LWAVWHGLQSLRYYRTRPTRFCSEFGFESLPNLNTIEKYSDEKDYSLKSKVFLAHQKCLS
GNKKMQFYITENFRLPKNFTDYVYLSQICQAECVRDATEYWRRNEGRCNGSLYWQFNDCW
PVCSWAGMDYYLEYKALQYEAKKFFQPVTISIDDDKDRIKVYAICDRETPCNLTVKASLR
TFDNDELFSAAATMNVEKFKPTVIFDFSTESLKKYDLKNTFLLLDAYEDDKKIARQTLLF
DKEKNLNLGNPTVTVDVEKDGDYAVYKIKSNYYVRKFALYQKYSSMPFSDNYFDLVKDEE
VVIIQEAKGISLDDLKNGLSTKDASKIEPCYSKFKDWLIKAKIFIEPVNFFNYIYYKWII

Enzyme Prediction     

No EC number prediction in MGYG000002027_00474.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	3	666	1.4e-100	0.6595744680851063

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	2.01e-84	1	628	11	632	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK10150	PRK10150	4.89e-12	70	418	86	417	beta-D-glucuronidase; Provisional
PRK10340	ebgA	1.56e-08	22	418	75	449	cryptic beta-D-galactosidase subunit alpha; Reviewed
pfam00703	Glyco_hydro_2	4.08e-06	214	287	34	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
pfam17786	Mannosidase_ig	6.93e-05	637	725	1	91	Mannosidase Ig/CBM-like domain. This domain corresponds to domain 4 in the structure of Bacteroides thetaiotaomicron beta-mannosidase, BtMan2A. This domain has an Ig-like fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCJ98156.1	5.84e-216	1	775	2	791
QNF27003.1	3.29e-184	5	793	6	801
AUG59052.1	1.90e-183	5	811	5	815
BBI32724.1	4.14e-183	5	791	6	802
ADU28568.1	3.12e-181	5	802	6	813

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VJX_A	3.20e-147	5	784	11	815	Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VJX_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VQT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VR4_A Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482],2VR4_B Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482]
2JE8_A	3.37e-147	5	784	13	817	Structureof a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JE8_B Structure of a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
7OP6_A	3.47e-147	5	784	13	817	ChainA, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP6_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_A Chain A, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482]
2WBK_A	9.12e-147	5	784	11	815	Structureof the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482],2WBK_B Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482]
2VQU_A	3.75e-145	5	784	11	815	Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQU_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q95327	4.16e-111	5	673	25	736	Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1
A1CGA8	5.80e-108	23	632	32	660	Beta-mannosidase B OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=mndB PE=3 SV=1
Q5B7W2	1.08e-107	22	632	31	660	Beta-mannosidase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=mndB PE=1 SV=2
Q29444	1.72e-107	5	673	25	736	Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1
Q0CCA0	4.09e-107	21	632	30	658	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2

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
1.000055	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002027_00474.