CAZyme Information: MGYG000001615_05247

Basic Information

• Species: Eisenbergiella sp900548905
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900548905
• CAZyme ID: MGYG000001615_05247
• CAZy Family: GH2
• CAZyme Description: Beta-galactosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
851	MGYG000001615_66|CGC1	97123.15	5.0464

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001615	6842156	MAG	China	Asia

• Gene Location: Start: 10971; End: 13526 Strand: +

Full Sequence      

MDEKQIGPEGRIDLNGTDWQMKEFVGMDWVWRDSVMPGTADVRWWYPAKVPGSVLHDLRE
NNLVPDPYYERNSLLVEWVPDRTWIYRKEFLVPGGLEGKRLTLVFEGIDYNSEIFLNGES
LGKQEGMYVPWSVDVTGKLCPGEKNLLAVVLEPAPFEQPQVGKTSLVSTHKSRMTYWWDF
CPRMIHQGIWQDVYLKVNREAILTDVYVHSVLAEDGAQALVHVELEADCPDGCLAEGSFG
DTPFRETVENGKCRICLTIEEPRLWWCNGQGEPYEYPVEVHLLDRQGRVSDCRKLDAGIR
SVEFLPNENGIAGREKEGSFTLCLNGRTIYMNGYNWVPADVMYGAVTEDTYVHLIRLAKE
AGVNILRVWGGGLIERDIFYRLCAKAGILVWQEFILSSSGIDNTPSEAENYTHFMRSQAE
SIIRQKRGFTALAVWCGGNELQEPDGTPLDEKNALVRTLGEQVRRLDGTRKWLPTSPSGG
VFLNSFENLEKCPEELFDVHGPWEHQGLHKQYELYNRGTCMLHSEFGVEGMTNYEALRRT
TAPEHFLPAGKDNPVYFHRGAWWNNEPLVQETFGGLSDIEEIRKGSQYMQYEGLKYAVEC
NRRRAFHNSGTFPWQFNEPYPNLYCTSSLDYYGNPKPAYYGVKKAYAPYLVTASFEGASL
WEKEWLEADIHAACNLPEGDRRGPIKVRARVYDMSGMLLQEEVFHLDSINMHSSRIGKLR
FLLARTDGELLLLRLALFAEGQDDMLAGNEYLFTKGRDLGAVFRMEKPVLTAQGINKGIR
LKNTGKSPALFLFLTNEKRVVTEPLGLVYWKDNYFTLLPGEERQILTDGEWKAACVQALN
MEYSSLDRFAQ

Enzyme Prediction     

No EC number prediction in MGYG000001615_05247.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	11	656	3.7e-81	0.6156914893617021

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	2.24e-58	47	659	31	642	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK10340	ebgA	8.67e-13	76	404	101	408	cryptic beta-D-galactosidase subunit alpha; Reviewed
PRK09525	lacZ	1.74e-09	86	390	124	410	beta-galactosidase.
pfam18368	Ig_GlcNase	3.10e-09	754	825	7	82	Exo-beta-D-glucosaminidase Ig-fold domain. This domain can be found in 2 glycoside hydrolase subfamily of beta-glucosaminidases (EC:3.2.1.165) such as CsxA, from Amycolatopsis orientalis that has exo-beta-D-glucosaminidase (exo-chitosanase) activity. It has an immunoglobulin-like topology.
pfam02837	Glyco_hydro_2_N	3.88e-09	37	195	16	165	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
AYQ72194.1	1.28e-254	11	828	4	834
AFZ65671.1	7.46e-234	11	842	2	840
BBJ37786.1	6.46e-204	11	825	2	809
QPP05544.1	4.52e-193	13	840	7	867
AXK31648.1	1.69e-192	12	834	6	875

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	5.09e-98	16	819	18	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	1.63e-71	45	826	25	815	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	1.68e-71	45	826	27	817	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	1.70e-71	45	826	27	817	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	4.27e-71	45	826	25	815	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
Q4WAH4	8.00e-60	29	651	13	658	Beta-mannosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=mndB PE=3 SV=1
A1D911	1.48e-59	29	651	13	658	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
B0YBU9	2.72e-59	29	651	13	658	Beta-mannosidase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=mndB PE=3 SV=1
Q5B7W2	9.07e-59	29	648	13	655	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
I2C092	2.57e-58	28	648	12	659	Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 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
1.000051	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001615_05247.