CAZyme Information: MGYG000001546_01913

Basic Information

• Species: Alistipes provencensis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes provencensis
• CAZyme ID: MGYG000001546_01913
• CAZy Family: GH2
• CAZyme Description: Beta-galactosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
802	MGYG000001546_5|CGC31	91989.23	5.6967

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001546	3805103	Isolate	not provided	not provided

• Gene Location: Start: 2420681; End: 2423089 Strand: -

Full Sequence      

MNTTFTKLTAALALLFAAGSLTAGEKSSLDGKWRLDYWPQGDTPIVSPADARQVEMKTID
ATVPGNVELDLLAAGLIEQPEIGSNVYDLRPWEGYQWRYSRTFTTPEHADGDHIQLNFNG
IDCYADVWVNGRQVGSADNMLIEHRFDITKALKPVGEENTLEVYIRSSVIEGRKYIPPTI
SFNFAQVESVYSRRAPHTYGWDIMPRLVSAGLWRGVELEVLKPVHLRDVHWFTTSVDVPN
KQAMVFLDYTITLPTALQDGKITTEFSLSRNGKQVAMYRAKVTSHAARHLLGLQDVDFWW
PRGYGEPALYDAEVKLMDEAGNTLDIDRRRIGIRTVKLDLTPTHTPENPGRFCFIVNGEK
IFARGSNWTPMDALHSRDTQWLERTFDLVTDLNCNMIRCWGGNVYEDSRFYELCDENGVM
VWQDFGMGCTFYSQREEFSRAIEREVTSVVMKLRSHPSIALWSGNNENDQTLAFGLLAPF
RMDPNRDVISRQVIPMVLYELDPTRSYLPSSPYLSEEVYRNGYAVQQLPEDHLWGPRGYY
KDPFYTTANCLFVSEIGYHGMPNRSSLEKMFPAETVYPWTDKKEFRWNEDWLTKAVRIFK
EWGYTPERNNLMINQVRLLFGEVPTKLDDFIFASQSVQAEAMKFFVEIYRGNKFAPKTGI
LWWNIRDGWPLISDAVVDYYFSPKMAYWFLRNVQRNVCVLVNDAADGSHPLVATNDTRSA
ANGTIRVSDVATGREIFRGSYTVGENARAEIARLPEMKGQGILLIEYTTPEGSFKNHYLY
GNAPFKLDEYRKLLRKTNIYDL

Enzyme Prediction     

No EC number prediction in MGYG000001546_01913.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	24	740	7.6e-93	0.6715425531914894

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	1.40e-63	28	718	14	653	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK10340	ebgA	3.10e-23	29	502	44	477	cryptic beta-D-galactosidase subunit alpha; Reviewed
PRK10150	PRK10150	1.06e-12	88	488	59	445	beta-D-glucuronidase; Provisional
pfam02837	Glyco_hydro_2_N	2.05e-09	28	152	3	122	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.
pfam00703	Glyco_hydro_2	1.52e-07	224	334	1	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNL40264.1	0.0	23	800	23	797
QQR15691.1	0.0	23	800	23	797
QRM99259.1	0.0	23	800	23	797
ANU59404.1	0.0	23	800	23	797
QUT78882.1	0.0	23	800	23	797

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	4.76e-94	61	743	46	700	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	2.25e-79	57	688	24	645	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	2.33e-79	57	688	26	647	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	2.37e-79	57	688	26	647	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	6.03e-79	57	688	24	645	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
Q0CCA0	1.69e-79	61	699	30	656	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
B8NW36	3.28e-79	63	699	32	658	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
Q5B7W2	4.46e-79	62	699	31	658	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
Q2TXB7	6.26e-79	63	699	32	658	Beta-mannosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=mndB PE=3 SV=3
A2QYN2	2.99e-77	63	736	32	709	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 SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000380	0.998809	0.000277	0.000188	0.000170	0.000152

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001546_01913.