CAZyme Information: MGYG000000170_01887

Basic Information

• Species: Alistipes_A sp900240235
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes_A; Alistipes_A sp900240235
• CAZyme ID: MGYG000000170_01887
• CAZy Family: GH2
• CAZyme Description: Beta-galactosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
807	MGYG000000170_5|CGC5	91594.93	5.3983

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000170	3119069	Isolate	China	Asia

• Gene Location: Start: 280014; End: 282437 Strand: +

Full Sequence      

MKKNRILGFCLSQLLLLGTVASASGATAPAAPVSLDGEWELSYWPQPEKAVTDPAALSGI
EVKTIPAKVPGNVELDLLAAGLIDDPMIGANVNKLRAWEGYQWCYTRRFDAPKLEPGQRA
ELWFGGIDCLADVWVNGKHAGSSADMLIERSFDVTDLIEQGGSNTVQVIIRPVVLGAQDH
LLGSFSMGNFATEESVYIRKAPHMYGWDIMPRLVSAGLWRGVELRTLNPARFTDVNWVTT
HVDTASRNVSLFVDFQTRLPFDQYDKAKVRFTLTRDGKEAYRGEQVLFAHAGRIVVNLEK
ADLWWPRGYGEPALYEAKGELIGADGQVLDTDVKRIGLRIVQLDLSDIHLPDERGKFCFI
VNGEKIFVRGTNWVPLDALHSRDAAQYESAMKLVTDANCNMVRCWGGNVYEDTRFFDLCD
ENGILVWQDFAMGCSFYPQRADFLDQLREEVTSVVLKLRNHPSLALWAGNNEDDANLFWS
RLQPFHLDPNRDQVSRHVIPEVLYEFDPTRPYLPSSPYYSEAVWEKGSLEQYLPENHLWG
PRGYYKDKFYTTAPCTFVSEIGYHGCPNRSSIEKMMTKQGVYPWTEGRKWNDEWITKSTR
RYEAWGPTMDRNNLMLNQVNILFGSVPDDLDDFVFASQSVQAEAMKYFVEMWRSRKFERT
GIIWWNVRDGWPIISDAVVDYYGSKKLAYYFLQNVQKNVCLLINDPVDGAYPLVAVNDTR
LPAEGTVTVTDVATGKEVFKGSYNVGPNGRQCVSNLPVMKGQGMLQIRYDANGESCSNHF
LYGEPPYKLKEYKGWLDKTKMYTNKDK

Enzyme Prediction     

No EC number prediction in MGYG000000170_01887.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	33	749	6.8e-84	0.6808510638297872

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	3.27e-64	34	736	14	670	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK09525	lacZ	2.28e-11	34	472	54	462	beta-galactosidase.
PRK10340	ebgA	1.63e-10	105	474	113	451	cryptic beta-D-galactosidase subunit alpha; Reviewed
pfam00703	Glyco_hydro_2	6.94e-09	230	339	1	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
pfam02837	Glyco_hydro_2_N	2.88e-06	34	170	3	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA23305.1	0.0	1	807	1	807
QNL40264.1	0.0	11	805	4	800
QQR15691.1	0.0	11	805	4	800
QRM99259.1	0.0	11	805	4	800
ANU59404.1	0.0	11	805	4	800

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	1.72e-103	33	719	27	675	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	9.83e-81	35	753	11	713	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	1.02e-80	35	753	13	715	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	1.03e-80	35	753	13	715	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	2.63e-80	35	753	11	713	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
A2QYN2	3.61e-79	69	749	32	724	Beta-mannosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=mndB PE=3 SV=1
I2C092	4.34e-79	28	690	2	651	Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1
Q5B7W2	2.35e-77	69	749	32	724	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	3.34e-77	69	749	32	724	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
B8NW36	1.13e-75	69	749	32	724	Beta-mannosidase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=mndB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000363	0.998832	0.000232	0.000207	0.000186	0.000166

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000170_01887.