CAZyme Information: MGYG000003012_01724

Basic Information

• Species: Blautia_A sp900540785
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A sp900540785
• CAZyme ID: MGYG000003012_01724
• CAZy Family: GH2
• CAZyme Description: Beta-galactosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
829	MGYG000003012_16|CGC1	97722.49	4.8495

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003012	3168635	MAG	United States	North America

• Gene Location: Start: 24669; End: 27158 Strand: +

Full Sequence      

MISLKLDTGWKMRETENGQWQTAVVPGTVYTDLLREGNMKNPFWKDNEDEICSLMEKDYE
YICQVQVSEKLLACNQVMLHFEGLDTLAEIYVNGQYAGEAKSQHRIWEYKVKELLHEGEN
ELRVVFRSPLKWIAEAYKKYGNIGNEDTYEGFMHLRKAHYMFGWDWGAHLPDAGIFRPVT
LLGINRGRLDSVYVRQEHEEGKVTLHFEPSVLREECSLKEKFSFRVKVISPEGEILSDKE
EQEISSVVIENPELWWPNGVGEQPLYTVSVTLFNEQGQEEDVWERRIGLRTMTMKREKDK
WGECFAHEINGKTIFAMGADYIPEDHLLGRRSEERTRRLLEDCKLANYNSIRVWGGGFYP
DDWFFDICDELGLVVWEDFMFACSVYELTPEFEENIRQEFIDNVKRIRHHACLGLWCGNN
EMEMFVDERCWVTKPSEVRDYLFMYERIIPEILKEYDPQTFYWPASPSSGGSFDEPNDPN
RGDVHYWKVWHGNRPFSEYRKFYFRYASEFGFQAFPSRKTLEEITDDPADMNPFSYIMEK
HQRNYGANGKIMNYMQQMYRYPNDFDRFIYSSQLLQADAIRYGVEHFRRNRNDNRCMGAV
YWQLNDCWPVISWSSIDYCGRWKALHYFAKRFFAPVLVSCQEEGWLTSEANMNRQHFGFE
KSIRLNVANETLKPRRIKVKWTIRDAFGNPVEEKMKAYKDICEKIVEVPPLSTVWLDKIE
LPEIDVFSEYVSFEGWEEDTCVSEGTVIFSYPKYFRYEDPKLTCTVQGDTIEITASAYAK
SVEILNETEDLLLSDNYFDMNAGTKKVKILRGEAKGLKLRSVYEGMENV

Enzyme Prediction     

No EC number prediction in MGYG000003012_01724.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	5	662	5.8e-101	0.6422872340425532

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	5.62e-89	75	672	80	681	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK10340	ebgA	6.27e-18	76	421	127	449	cryptic beta-D-galactosidase subunit alpha; Reviewed
pfam00703	Glyco_hydro_2	6.02e-11	188	290	2	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
pfam17786	Mannosidase_ig	2.13e-08	663	754	3	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.
pfam17753	Ig_mannosidase	1.49e-07	759	824	1	78	Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWY97345.1	0.0	1	824	1	809
ANU78706.2	0.0	8	824	38	847
ASU31771.1	0.0	8	824	38	847
QBE96379.1	0.0	2	824	26	839
QMW80334.1	0.0	2	824	26	839

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	5.82e-145	1	805	24	805	Crystalstructure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_B Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_C Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_D Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12]
2VJX_A	1.76e-142	6	639	11	657	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	1.86e-142	6	639	13	659	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	1.91e-142	6	639	13	659	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	5.02e-142	6	639	11	657	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A1CGA8	1.90e-113	6	816	9	834	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
Q4WAH4	7.25e-113	6	818	9	832	Beta-mannosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=mndB PE=3 SV=1
Q0CCA0	9.67e-113	6	825	9	842	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
A1D911	1.01e-112	6	818	9	832	Beta-mannosidase B OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=mndB PE=3 SV=1
B0YBU9	2.76e-112	6	818	9	832	Beta-mannosidase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=mndB PE=3 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
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003012_01724.