CAZyme Information: MGYG000001689_04442

Basic Information

• Species: Blautia coccoides
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia coccoides
• CAZyme ID: MGYG000001689_04442
• CAZy Family: GH2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
838	MGYG000001689_21|CGC1	97910.52	4.9369

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001689	6086770	Isolate	United States	North America

• Gene Location: Start: 71247; End: 73763 Strand: -

Full Sequence      

MFELKMNDNWRMHESLLSVEKDQWAYVHGLEDGWYSCSLPADVRMPLIENGVIRDPVLAD
YCRESEWIEKRAWWFERTFDGCSVDKNEDIIELILEGLDSKSDIFINGQYIGSHYSVHYP
FVYDIKDKIKEGENVITVRVTSGLESVSDQDLSELNHAVCLETDNGGKYRGDARRAFVRR
PQYTVGWDWGPKVITCGITGGARLEGHKKIALREVCLHTEEIGEQAKLKLMLNVENLGFI
SSRDGKYKVRISYEGDTVFEQIYEDRLFTSGYNYFEEEILIPHAKLWWPNGYGRQPLYEV
QVEAVCEDAVEIYPAFRYGIRKLELNTDVLKGKDRKFQFVINGKPIYCKGGNWIPNDFIY
ARVTDEKYRVLTEEAAEANFNMLRIWGGGLYERDIFYDLCDEKGILIWHDFMFACSTYPD
HHQWFREEMRREFDYQTKRLRSHSCLGLFCGTNEVHWLFNSTDNPKWGIEFTYEHQYGMY
IANILSKEVIHANCPFIPYWNSSPYGGELPNDDTVGDIHHWQQAYMSKKMEERIEAKDYD
KIKAKFVSEYGYVGPCCMETILEYMDGQPLDRTSEVWQMHNNVFEKDTVNTAIEKNYVDH
ADRLSLEDYITYAGMVHGMMYGYSLESMRFKEQCYGGLFWMYNDAWGEVGWTIIDYYLRR
KIAYYGVKRALAHQKFTMRTEDGSVILQGANDTPKPLSVTAEFGYVSFDGTIRETRKIQL
ETEPGERSYLLREALPDRDYKKGTIMLYVLDENIDNIWLRLDDMRNLDFEKSQVICTEDR
QEGNDRILTLNSESFAHGVHVKGNYRCSDNYFDLLPGETKTIIVRGAKETALQMASVR

Enzyme Prediction     

No EC number prediction in MGYG000001689_04442.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	5	729	1.1e-79	0.6835106382978723

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	4.40e-53	28	695	28	655	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
pfam17753	Ig_mannosidase	2.70e-08	775	833	4	65	Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.
pfam02837	Glyco_hydro_2_N	3.49e-08	74	140	68	133	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.
PRK10340	ebgA	3.52e-06	75	407	113	394	cryptic beta-D-galactosidase subunit alpha; Reviewed
PRK10150	PRK10150	3.66e-06	246	407	203	352	beta-D-glucuronidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QMW77011.1	0.0	1	838	1	838
QIB55134.1	0.0	1	838	1	838
QBE99829.1	0.0	1	838	1	838
QBE97186.1	0.0	1	838	1	836
BBI35730.1	3.28e-264	3	824	2	824

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	3.00e-124	23	816	32	802	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	1.28e-95	24	824	15	816	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-95	24	824	17	818	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	1.36e-95	24	824	17	818	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	3.50e-95	24	824	15	816	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
Q5B7W2	1.33e-80	32	830	24	832	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	4.26e-77	31	828	23	832	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	4.01e-76	31	828	23	832	Beta-mannosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=mndB PE=3 SV=1
Q2TXB7	7.48e-76	39	828	32	831	Beta-mannosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=mndB PE=3 SV=3
B0YBU9	1.44e-75	31	828	23	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
1.000032	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001689_04442.