CAZyme Information: EPE09564.1

Basic Information

• Species: Ophiostoma piceae
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Ophiostoma; Ophiostoma piceae
• CAZyme ID: EPE09564.1
• CAZy Family: GT2
• CAZyme Description: Beta-mannosidase [Source:UniProtKB/TrEMBL;Acc:S3C7R2]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
910		102096.53	4.6601

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_OpiceaeUAMH11346	8884	1262450	0	8884

• Gene Location: location=KE148147:1864414-1867146(-)

Full Sequence      

MVLLPPRLDDPTTDDQAVPLLNNTSSGIMAFHSLTVDQGWQFKQADAEETSGVGEWRSVG
QFPTNVHLDLLAHKLIPDPYIGKNEEAVQWIGERRWVYKASFVTPPASSAAGAASVLAFD
GLDTFATVVLNGHTILESDNMFIPYRVDVTSSLSPAGKENTLEITFDSAYLRGWQLVDKY
PDHKWGCWNGDSSRLAVRKAQYHWGWDWGPALMTCGPWRPIRLETYTSKIADLSFETVVD
KSLASATVKANVEIETLGTAPSSSPRVRIDVSLGDVAVASETVATVATKNDKGDSTATIT
TAAAAFHISSPALWYPARYGEQPLYTVRATLLADTTDEPAHEISKKIGLRRAELIQRPIK
DQPGTSFFFEVNNIPIFSGGSDWIPADNFIPRISDSRYYDWVKLALDGNQVMIRVWGGGI
YEEQAFYDACDELGVLVWQDFMFGCGNYPAWPELRESIRLEAEVNVRMLRHHPSIVIWAG
NNEDYQYREEQNLEYDYANKDAESWLTTDFPARYIYEKILADVCSSLIPDTYYHYGSPWG
GGVDTHDPTVGDTHQWNVWHGSQERYQDFDKLVSRFVSEFGMEALPHIKTIDAMLPLGRR
DPDRYAQSSTLDFHNKATGHERRLALYLVENMRYGPDPLEQYVYYTQLMQAECLASAYRL
WKRQWKGPGREYCGGALVWQLNDCWPVTSWSICDFYLRPKHSYYTVKREMAPLTIGITRS
ETEKVVGSNPHSRVDVKKETTIEIWGSNLTVEDLAGVDCVVRAWDVETGQQTYEKTVEAG
IVLEANRSTELAAFAVPGEPGHEARTVVAAYLEKDGKQLARYVNWPEPLKYLHLPEPKDL
SVVLSADGTGVEISSSVPIKGVAIELEDDEAEEDVVRFDDNLIDIVPGETVTIGVTGATS
ATKFKARYLQ

Enzyme Prediction     

EC	3.2.1.25:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	33	811	5.2e-91	0.7180851063829787

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225789	LacZ	2.10e-68	35	707	14	627	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
407658	Mannosidase_ig	6.82e-15	740	831	1	91	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.
395572	Glyco_hydro_2	1.53e-08	230	350	3	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
407625	Ig_mannosidase	0.003	841	902	7	63	Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UQC87618.1|GH2	0.0	34	909	32	873
AEO69937.1|GH2	0.0	34	909	7	848
EAA35570.1|GH2	0.0	34	909	7	851
AFJ59925.1|GH2|3.2.1.25	0.0	34	909	7	852
VBB71464.1|GH2	0.0	36	909	11	851

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	2.37e-126	26	908	19	814	Crystal structure 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	3.77e-112	34	896	9	817	Structural and 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	3.95e-112	34	896	11	819	Structure of 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	4.04e-112	34	896	11	819	Chain A, 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	1.05e-111	34	896	9	817	Structure of 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
sp|I2C092|MANBB_THETO	0.0	34	909	7	852	Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1
sp|Q0CCA0|MANBB_ASPTN	6.77e-278	30	909	3	841	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
sp|A1D911|MANBB_NEOFI	1.45e-277	36	897	9	830	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
sp|Q4WAH4|MANBB_ASPFU	1.17e-276	36	897	9	830	Beta-mannosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=mndB PE=3 SV=1
sp|B0YBU9|MANBB_ASPFC	1.66e-276	36	897	9	830	Beta-mannosidase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=mndB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999735	0.000306

TMHMM  Annotations     

There is no transmembrane helices in EPE09564.1.