CAZyme Information: MGYG000003849_00128

Basic Information

• Species: CAG-475 sp900547975
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-917; CAG-475; CAG-475 sp900547975
• CAZyme ID: MGYG000003849_00128
• CAZy Family: GH2
• CAZyme Description: Exo-beta-D-glucosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
860		99003.05	7.708

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003849	1745620	MAG	United States	North America

• Gene Location: Start: 148385; End: 150967 Strand: +

Full Sequence      

MYKKNRKNFIDLCGQWTLLDPVSRKEYPATVPSCNYSDLQNAGVIPDPFVALNEKKTEWV
SKQDWVYEKTFDLTREDLFADRIFLNFEKIDTLCDVTLNGEKIASVSNCHIPYSFEVKSF
LKEGENKLSLFFPSPVNAVIQKQKRIKCPVNSNGLTGIAHLRKPQCHFGWDWGPVIPVSG
IEGDVKLVFSNKGRILQTRVRQISEDGGVKLRAEIQNEIYSDDTLELDIKLVCPRGETYE
ARAVAKDKNIVEFLVEKPLLWYANGMTNCHEQPLYTIETTLLSSDCVLSSSKKQVGLRTI
TLDRSRDKYGSNFCFYVNGKRVFAKGANWIPTDSYPTKTTKEDIEEYVKIARDSGFNMLR
VWGGGGYESECFYDLCDRYGILVWQDLMFACQAYPFFDDEFLQSVKEEVKHVVNRLADRA
CLALWCGNNEIEAMTAGWATRRKFVKWTKTFFYDILPSELKKYDDVTPYVEGTPIGTKFL
KKVGSDNVGDVHLWAVWHGFQPLAYYKTRNPRFCSEFGFESMPDLKTIAKFASEADFDLS
SKVFSAHQKCRGGNEKMKYYIAERFRLPKRFEDYVYLSQLCQSLCVGEATEHWRATERCN
GSLYWQFNDCWPTCSWSGLDYYKNYKAVQYEAKKFCAPFSLAIEREKNDVKVVVFNDNIA
SQKCVLDVKVETFDGKELFFEQIPVEVDGCSTAVAKQYDVRKFGGKKALKNAVFVATLTC
ENPQNVAQCQPETIRQTMLFGKEKNLNLPKANVTVDVHREGNKAIYTIKSDAYVRKFALF
TKQNSPLSDNYFDVLPNETVHISQTIDEGCALEVLKNNFEFKHVATIEPKSSKFADSFFR
FKTLLSTWNLLNYIWYKFFM

Enzyme Prediction     

No EC number prediction in MGYG000003849_00128.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	3	703	1.5e-100	0.7074468085106383

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	5.51e-90	9	638	12	631	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
PRK10340	ebgA	2.37e-08	35	383	89	394	cryptic beta-D-galactosidase subunit alpha; Reviewed
pfam00703	Glyco_hydro_2	8.24e-07	194	298	2	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
pfam17753	Ig_mannosidase	6.51e-06	750	825	1	77	Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.
pfam17786	Mannosidase_ig	1.71e-05	648	728	1	81	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
BCJ98156.1	1.80e-202	12	858	6	855
BAJ62595.1	9.97e-179	16	813	14	814
CUS03525.2	8.83e-172	12	809	6	800
AUG59052.1	2.96e-168	10	822	3	812
QGH33887.1	1.08e-163	10	798	4	783

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	3.30e-146	10	796	27	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]
7OP6_A	4.88e-141	16	823	17	844	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]
2VJX_A	8.89e-141	16	798	15	810	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	9.37e-141	16	798	17	812	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]
2WBK_A	1.28e-140	16	823	15	842	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	7.00e-104	30	652	31	669	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
A1CGA8	2.88e-100	31	652	32	669	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
Q2TXB7	2.86e-98	31	652	32	669	Beta-mannosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=mndB PE=3 SV=3
B8NW36	2.86e-98	31	652	32	669	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
I2C092	5.01e-98	21	802	27	836	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
1.000056	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003849_00128.