CAZyme Information: MGYG000000441_00507

Basic Information

• Species: CAG-312 sp900545705
• Lineage: Bacteria; Verrucomicrobiota; Verrucomicrobiae; Opitutales; CAG-312; CAG-312; CAG-312 sp900545705
• CAZyme ID: MGYG000000441_00507
• CAZy Family: GH2
• CAZyme Description: Beta-galactosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
811	MGYG000000441_3|CGC3	92020.04	8.9369

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000441	2454454	MAG	Sweden	Europe

• Gene Location: Start: 84678; End: 87113 Strand: -

Full Sequence      

MKNLIKKFPQTVAVLAAIAAIFLFFGSRERTVQPSQKASNAGGTDLNGQWSLKFWPQPDT
GALRTLGGAKTAQGAKTIKAQVPGNVELDLFKAGLVPNPELGDNSYKLREYEGYQWLFSR
EFTSPNLGSGERAILRLDGVDTFADIFINGKKVGETSNMLIPHTFDITDFLSKGGKNNLD
ILIRSAIMESNGRKIGAISSAYDSEGIRKAPHMYGWDIMPRMLSAGIWRDAKIEIQKPAR
IEDIFFMTVYTDPKNNEAVCSARIRTALPRELLGKLSVLAKLSIGGETVWSRKMPADMFT
LSPRDIKIKNAKLWWPRGYGESPLYVFEASLLSPDGKLLDSKRINVGLRTVSLKRSDVFK
NGDKGEFAFYVNGRKIYIKGTNWVPLDALHSRDPQHLQKTLEMAADLNCNMLRCWGGNVY
ESDAFYDFCDKNGILIWQDFSLACTTPPQDDDFAKAMEIEARSVVERLRSHPSLALWAGN
NENDSSFDWLFNSNRLNIDPSKERISRKVLPGVLYELDPTRPYLPSSPYYSNDVFENKAD
PSEVHLWGPRGYYKAPFYTSSNAHFVSEIGYHGCPNRESLEKMFDKEHLYPWTDAKNLKW
NKQWQAKAITPFESNIGSEKRNYLMTNQIAKVFGEVPRDLDDFISASQIVQAEAKKYFIE
FWRTGKPYRCGILWWNLRDGWPILSDAITDYFFSKKLAYYYIKRVQENAIVAVNDALEVI
AVNDTFKPAEGKVEISDIEGGKVLFEANFKIPPNGKTLIGNVSGLPSERGMLLIKYEIDG
KEQLNHYLYGKPPFDLKKYRKWAESLEIKRD

Enzyme Prediction     

No EC number prediction in MGYG000000441_00507.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	35	716	9.3e-91	0.6263297872340425

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	2.46e-65	44	713	13	637	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK10340	ebgA	2.70e-16	117	484	112	451	cryptic beta-D-galactosidase subunit alpha; Reviewed
PRK10150	PRK10150	1.10e-14	108	522	60	444	beta-D-glucuronidase; Provisional
pfam02837	Glyco_hydro_2_N	1.90e-08	46	174	4	125	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	2.25e-07	239	349	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
QGA23305.1	2.00e-264	41	808	30	801
QNL40264.1	1.14e-256	38	805	21	793
AGB28636.1	1.55e-256	46	808	29	796
QQR15691.1	9.16e-256	38	805	21	793
QRM99259.1	9.16e-256	38	805	21	793

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	2.35e-107	70	794	36	749	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	1.77e-86	76	754	24	708	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	1.83e-86	76	754	26	710	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	1.87e-86	76	754	26	710	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	4.79e-86	76	754	24	708	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	1.44e-75	80	704	29	655	Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1
Q0CCA0	8.15e-75	80	735	30	680	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
Q5B7W2	5.19e-73	82	781	32	752	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
A2QYN2	7.25e-73	82	810	32	780	Beta-mannosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=mndB PE=3 SV=1
A1CGA8	6.84e-72	82	757	32	726	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

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
0.941772	0.056169	0.001402	0.000170	0.000098	0.000412

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000441_00507.