CAZyme Information: MGYG000000184_03089

Basic Information

• Species: Blautia_A luti
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A luti
• CAZyme ID: MGYG000000184_03089
• CAZy Family: GH2
• CAZyme Description: Beta-galactosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
849		99022.27	5.1114

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000184	3628099	Isolate	China	Asia

• Gene Location: Start: 14872; End: 17421 Strand: +

Full Sequence      

MKTIKLNGIWELSEGNDHSLCQVQVPGTVLSGLLNAGKIEDPFYRTNEEQTRKLFWKDYV
FERSFSVEADLLTEDQILLICEGLDTLTDIYINDHLIAATDNMHRTWKFPVKEYLKEGEN
QIRIIFHSVLQYIENYTYAEHKEIHYVPCGGMKGNQLLRKAHSMFGWDWGPQTIDAGIFR
DIYLEGFSHPRMEDIIFHQKHQDGKVTVTAEIQLGKKNISLNNCCDHTVSNTVSPDYKYE
NYTVNIEISGPDYTRNQTLTAGQNGRVTFTFDIENPHLWWPNGYGKQPLYNVTVTLRSNT
DNILETVNRRIGLRTLTISQEKDQWGSEFAFCVNGLKIFTRGGNYIPEDCLYTRISHETQ
KYLLESCKRANFNCVRVWGGGYYPSDHFYDLCDEMGLIVWQDLMYACNVYDVTKAFGESC
RQETLDNVKRLRHHASLGLWCGNNEIESAWNHWQDFQTETPYLRADYVKLFEDILPDAVK
ETDQDTFYWPSSPSSGGCFDNPDDENRGDTHYWDVWHGQKPFTDYQKYHFRFCSEFGFQS
FPCMKTVESYTEEKDRNIFSRVMESHQKNDAANGKILYYLSENFQYPHDLNHLLYVSQIL
QGMAMKYGVDHWRRNRGRCMGTLYWQVNDNWPVASWSSIDYFGRWKALHYMAKKFYAPLA
VSMRKDGEIFRAYLENETAQTQEWTATISVKNMKCEILDSVQAAGSTTPFKAEEIIQIDV
SNWKKQEDYVFVETVLKLSDGTVLTDTETLVPYKYVELETPEINIDVEEQKDTYLLKIKA
NCFVPFLSLDFKDADVTLEDNFFHITDTEEKVIRADKKDIWNGSFKNAQDMKNRLEILTL
IPVKDGVRN

Enzyme Prediction     

No EC number prediction in MGYG000000184_03089.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	3	780	6.4e-110	0.7726063829787234

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	5.88e-104	1	684	10	659	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK10340	ebgA	1.29e-20	60	399	112	394	cryptic beta-D-galactosidase subunit alpha; Reviewed
pfam00703	Glyco_hydro_2	2.04e-10	191	314	2	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
pfam17753	Ig_mannosidase	2.24e-09	761	840	2	76	Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.
PRK10150	PRK10150	0.001	176	399	168	352	beta-D-glucuronidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCU02115.1	0.0	1	840	1	824
CBL20579.1	0.0	1	840	1	838
CBL08662.1	1.90e-292	6	815	9	828
VCV23589.1	5.41e-292	6	815	9	828
CBL13897.1	2.24e-290	6	815	16	835

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VJX_A	1.26e-157	10	813	15	814	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	1.33e-157	10	813	17	816	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	1.37e-157	10	813	17	816	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	3.60e-157	10	813	15	814	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	1.50e-155	10	813	15	814	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
A1CGA8	1.66e-112	25	811	32	824	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
Q29444	1.91e-111	3	807	22	848	Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1
Q95327	2.82e-109	3	807	22	848	Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1
A1D911	6.97e-109	25	666	32	663	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
Q5B7W2	6.86e-108	10	813	13	824	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

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
1.000051	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000184_03089.