CAZyme Information: MGYG000002330_05135

Basic Information

• Species: Eisenbergiella tayi
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella tayi
• CAZyme ID: MGYG000002330_05135
• CAZy Family: GH2
• CAZyme Description: Beta-galactosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
845	MGYG000002330_150|CGC1	97535.56	4.7787

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002330	7416064	Isolate	not provided	not provided

• Gene Location: Start: 21571; End: 24108 Strand: +

Full Sequence      

MLSLNGKWKVTHVPYCSPIDFILSPSFVPEGWLDAAVPEEIHRTLRNAGIIRGNVYGKTD
EEELWIEQADWIYHKEFFVPAEETGRQVLLTFEGLDTFCDIYLNGILTGSHKNMHIPFQT
DVKDLLHFGGRNVLVVRFYSPVRYVENRDDSEIFSITTSDRIFARKAQMNYSWDFCGRCV
TVGIWKNVSLTAVDSVRISSHYLYTKLLEEDSALLHLNIDFTTPDYDTFSSYYVSVNIEK
DGNPVCHISERAADCSVLEFSLEAPILWWPRPYGEPFLYDFVLRLEKEGQILQEIRQKFG
IRRIAVLQEPVEDGLSFQFAVNGRRLFIRGANWVPLNTIYTDITDEDYEKAVRYACEGNL
TMLRIWGGGIYESPRFFELCDEKGILVWNDFMFACGIYPRDEEFLENVALEAEAVIKKYR
NYTSLALWAGDNENGQAYGWAGRPYEFAEDPISYRILKKACETFDPNRFYLTTSPGSPCG
DLKGGDNPESPYQGDSHLYIMSADPGIRSGRDYGRNYYKRILSYRPRFMSEFGFICFPEK
DTFYRYNFQRLPLSRENELTEFLPFTEEFMEKNDFDSAIYYSQVYNSMALKYWIEYFRSL
KGICSGTLYWKFNDPAADCAKGGIFPSHMSVIDMFGQPKMTYYYTRRAYEDFLVCCTEKK
DAFRIHACSELTEEIKGTLHITHMDFKGKVILEKSMACTASADSTTLLAEFPGCTFAVKD
KYEEYFRIRFDTSGCEYENRYFFADICEINRLKLPPAGLRIRKASFEDGNIRLYLYTENF
ARSVRLRLSDRSAGFADNYFDMDADSEKIVCVIPDDKDGLEAAALIIDGINVSSILLPLA
SLLSV

Enzyme Prediction     

No EC number prediction in MGYG000002330_05135.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	2	679	1.8e-101	0.6502659574468085

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	1.84e-65	3	651	14	631	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK10340	ebgA	5.36e-22	2	468	42	470	cryptic beta-D-galactosidase subunit alpha; Reviewed
pfam00703	Glyco_hydro_2	7.65e-13	196	302	1	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
PRK10150	PRK10150	1.02e-12	73	330	69	296	beta-D-glucuronidase; Provisional
pfam17786	Mannosidase_ig	1.64e-09	661	745	1	88	Mannosidase Ig/CBM-like domain. This domain corresponds to domain 4 in the structure of Bacteroides thetaiotaomicron beta-mannosidase, BtMan2A. This domain has an Ig-like fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNK54904.1	1.59e-118	2	812	9	824
ALS99783.1	5.02e-118	30	802	27	801
ACI19676.1	2.94e-116	1	799	3	774
AEH49566.1	1.37e-115	2	835	1	831
ACL70061.1	7.69e-115	2	802	1	801

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	3.83e-116	1	799	26	797	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	3.92e-113	30	821	23	826	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	4.11e-113	30	821	25	828	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	4.20e-113	30	821	25	828	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	1.09e-112	30	821	23	826	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	2.57e-86	29	696	23	713	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
Q0CCA0	1.58e-81	30	694	24	710	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
A1D911	1.63e-81	9	681	3	698	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
B8NW36	4.03e-80	29	681	23	698	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
Q2TXB7	5.57e-80	29	681	23	698	Beta-mannosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=mndB PE=3 SV=3

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
1.000066	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002330_05135.