CAZyme Information: MGYG000002232_01889

Basic Information

• Species: Eubacterium_R sp900539845
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; Eubacterium_R; Eubacterium_R sp900539845
• CAZyme ID: MGYG000002232_01889
• CAZy Family: GH2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
816		93690.61	6.8441

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002232	2282853	MAG	United States	North America

• Gene Location: Start: 21010; End: 23460 Strand: +

Full Sequence      

MKTISLNGNWQMTMPGGKTYGAEVPVSDYNVLLKNGVIDDPFYGTNENDSLYIGETDKSF
SRKFSLEKDFLENENIMLQCDCLDTLAEIYINGSLAGKSQNAYIGFEKDIKKFVNEGENS
IEIRFSSPVEYVKRRQKEKALPRNANGINGVPYIRKPACHFGWDWGINMPLSGILGNIRL
IAFHDEIRDFSLNQTHKDGVVTLKIHTDIKKDSSGELTAPDGEKRTFKIEDGYAQITIET
PELWWTRELSGRDKQPLYTVKIENTAKRIGLRTIELDRSKDKYGSNFRFILNGVPIFAKG
ANLIPPDAMADRINKASFEKITNDAILANFNMLRVWGGGYYGSDEFYDLCDEKGILVWQD
FMFACLMYPFYEEDFLANVLNEVKYNVSRISHHASLALWCGNNEIEFMFTYLPENSEIVK
WYRKFFYDILPGELRKYDKKTPYIETSPIGAGFRKNITADKCGDTHMWHVWHGCKDLKYY
TKRYTRFMSEYGMESLPSKDCIEQFAEKEEMNLFSETMLSHQKCLSGNAKMRYYLLERYN
EPDRFDDLIYLTGLIQSQCVGNAAEHFRRCKGRCNGALWWQLNDCWGCPSWSSVDYSGKW
KPLMYEGKRFFSPVALSVKEKGSNAEIYLLNDTLESAEYTVTAKIRDFQGRIFAEESEKV
FSAAGNPLKAITVSLKGTDKIRNVLQAELYNAEGKKIFEKTTVFAPERKLDLKRAKIRVL
VDGNQLTLECNTYARSVFVDIKGESTPLSDNSFDLIPGEPKTIRLEKECRIKPESISVKC
VNNVRSSSTEAERTAYRVGFSLKPENIANMFYYTFS

Enzyme Prediction     

EC	3.2.1.25

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	2	714	4.1e-92	0.7473404255319149

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	7.07e-76	1	768	10	787	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
pfam17753	Ig_mannosidase	2.59e-12	715	783	6	78	Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.
PRK10340	ebgA	2.28e-11	4	357	74	394	cryptic beta-D-galactosidase subunit alpha; Reviewed
pfam17786	Mannosidase_ig	5.45e-10	623	706	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.
PRK10150	PRK10150	9.93e-08	71	497	79	515	beta-D-glucuronidase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AUG59052.1	1.03e-191	4	768	3	794
BCJ98156.1	2.65e-189	5	755	5	791
QNF27003.1	1.45e-175	1	768	1	796
QTE69834.1	1.74e-174	1	785	1	811
QTE73768.1	1.74e-174	1	785	1	811

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VJX_A	7.48e-136	2	790	7	840	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	7.87e-136	2	790	9	842	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	1.59e-135	2	778	9	831	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	4.18e-135	2	778	7	829	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]
2VQU_A	8.62e-134	2	790	7	840	Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQU_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q29444	2.96e-101	3	614	22	691	Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1
Q95327	1.55e-100	3	645	22	722	Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1
Q8K2I4	2.20e-98	3	756	22	847	Beta-mannosidase OS=Mus musculus OX=10090 GN=Manba PE=1 SV=1
O00462	3.09e-96	3	646	22	721	Beta-mannosidase OS=Homo sapiens OX=9606 GN=MANBA PE=1 SV=3
Q4FZV0	2.31e-95	3	614	22	691	Beta-mannosidase OS=Rattus norvegicus OX=10116 GN=Manba PE=2 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
1.000070	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002232_01889.