CAZyme Information: MGYG000003412_01986

Basic Information

• Species: HGM12789 sp900766585
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; HGM12789; HGM12789 sp900766585
• CAZyme ID: MGYG000003412_01986
• CAZy Family: GH2
• CAZyme Description: Exo-beta-D-glucosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
849	MGYG000003412_51|CGC1	94912.76	5.3231

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003412	2381083	MAG	Fiji	Oceania

• Gene Location: Start: 26752; End: 29301 Strand: -

Full Sequence      

MNVSLNGSDWVLTGWNRHQWKFYKIRETGGLSRPMVALIPAQVPGSVQTDLLRAGVIEDW
NRGKNFLAAEWVEHREWVYEKVFTVTKAQQSVHSRLCFEGLDFAGHVFLNGERLFSFDQM
HRPYETDVTGRLTAGENHLRVVLLQPPEVDGQVGYTSKTTVLKSRYNYGWDWMPRLVNIG
IFGAVTLRFAESAVLKNVYPKAAVEPDGTGVLLLTADVEGLCDRMLSVRYTVSQDGGCVA
SGTVPVTVKAGKTVPLVQTVRIENVRLWYPAGMGQQPLYTVELQLLDNDTVPGDCFSGQV
GFCTITYSQPEGAAEYHLPYAVTVNGDWMPIKGMNWVPISPFYGSVTEEDYRYYLGQLLP
CGINLLRIWGGALLESETFYRLCDEQGILVWQEFPQSSSGIDNAPCEEPAFVQTLCEMAE
WYLRRRRHHVCLAFWCGGNELYDAAYRPVAKESGNITALAKTVQEWDPDRLFLPTSPSGP
VASWSRGMTSPEQCGDTHGPWLYEGPREQCYRFNHDRSLLHSEVGAPACPRLESLKKYAD
HPIWPFDERDSYWLNRGAWWIYNEELIGLFGEFEPDDNGLSDYVRAYRYTQMEAIRYAAT
SIRRAGKRKAGLIVWMANEPFPNSANTSLLEYDGCPKPAYYKLKNAFAPVSLGLGYETPA
MRSHGGRQVEVYAFSDRETVLHDVTVEVFDCRGSSLKRVEYGTVRVSYTETIGELTLPGV
PPLILVRLTAAGEQPVCEEYVFTINGRTPFGALLALDCAPMAVTRASDCRFLVKNTGKTV
ALYVDAVGKDAAGRPLVMEGSGRCLLPGEGVEIFSVQPCAELTVETLNRTREQAEEEAVR
ALRSVGAGK

Enzyme Prediction     

No EC number prediction in MGYG000003412_01986.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	40	698	9.9e-72	0.6329787234042553

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	8.75e-49	19	683	18	659	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK10340	ebgA	4.60e-11	78	471	112	471	cryptic beta-D-galactosidase subunit alpha; Reviewed
PRK09525	lacZ	1.22e-07	79	454	124	490	beta-galactosidase.
pfam00703	Glyco_hydro_2	9.99e-06	195	302	3	105	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
pfam02837	Glyco_hydro_2_N	1.53e-04	78	145	68	135	Glycosyl hydrolases family 2, sugar binding domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNK55904.1	4.34e-194	3	817	5	834
QGQ98314.1	3.06e-191	5	784	7	806
AEE97200.1	7.89e-189	2	813	4	824
QTH43255.1	6.40e-183	2	822	3	842
QNK59485.1	1.81e-170	14	829	2	822

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	1.21e-64	41	654	46	660	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	8.84e-64	39	706	26	705	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	9.05e-64	39	706	28	707	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	9.16e-64	39	706	28	707	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	2.26e-63	39	706	26	705	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
I2C092	1.00e-58	41	717	29	726	Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1
Q5B7W2	5.91e-52	20	657	13	663	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
A1CGA8	1.79e-48	43	657	32	663	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
A1D911	1.40e-47	21	657	11	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
A2QYN2	6.04e-47	43	657	32	663	Beta-mannosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 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
1.000026	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003412_01986.