CAZyme Information: EJT77977.1

Basic Information

• Species: Gaeumannomyces tritici
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Gaeumannomyces; Gaeumannomyces tritici
• CAZyme ID: EJT77977.1
• CAZy Family: GH5
• CAZyme Description: Beta-mannosidase [Source:UniProtKB/TrEMBL;Acc:J3NP74]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
880		98611.31	4.8906

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GtriticiR3-111a-1	14749	644352	291	14458

• Gene Location: location=GL385396:1659114-1661768(+)

Full Sequence      

MAPSRKVIPLDKGWEFRQADKKDAEFLPVAQFPTNVHLDLLAHGLIPDPFVGKNETDVLW
IGEAQWTYRTTFSTPAPPSGSDGGARAVLAFDGLDTFATVLLNGAKILETDNMFVPERVD
VTGALREGGGDNELVIHFDSAYLRGWKLVEKYPDHKWGCWNGGNSRLAVRKAQYHWGWDW
GPALLTCGPWRPIALELYAGRVADLHVDVDVPESLDSATAVAHAVVEGAGDKVRFEISLR
GSVVAAETVQAVPVDSKAVSGAASATFHIQKPALWYPIRYGEQPLYTVKAILLVSDDETS
AAAEIDTASKRIGLRRAELVQQSLTDQPGTSFFFRVNNVPVFCGGSNWIPADSFIPRVST
NRYRDWVKLVADGNQFMIRVWGGGIYEEQALYDACDELGVLVWQDFLFGCGNYPTWPELL
DSIRREANENVKLLRHHPSIVIWAGNNEDYSYAESVKLTYNYADKDPENWLKTDFPARYI
YEKLLPDVCADLVPRTYYHPGSPWGGGVESSDPTVGDLHQWNVWHGKQEKYQNYDKLVGR
FVSEFGMEAFPSVRTIDQYLPLGKLDPDRYPQSSMIDFHNKADGHERRIALYLVENMRYG
PDPLEHFVYSTQLMQAECLSSAYRLWKRQWKGPGREYCSGALVWQINDCWPVTSWAIADY
YLRPKMAYFAVKREMAPLTVGITRREDKTARDEHTRVVIKVEAWACSLKLEEVTVDVLLR
AWNVETGEQTYEEKVAEGLVLQGNRSTELLSREVPLKSKDGSSTDNNDNLEEAGRTVVAV
YLVDAATGEQLARYVNWPEPLKYLHLQKPKELAARLVSGGTAVEISAEVPVKGVALESED
DGVKFEDNLIDIVPGEVVKVGVRGADEGTVVTTRYLGMLD

Enzyme Prediction     

EC	3.2.1.25:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	3	735	6.5e-94	0.675531914893617

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225789	LacZ	7.33e-86	3	672	8	627	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
407658	Mannosidase_ig	6.32e-10	700	803	2	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	2.72e-08	201	315	2	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
407625	Ig_mannosidase	1.24e-05	817	870	11	64	Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.
397119	Glyco_hydro_2_C	0.003	392	583	65	247	Glycosyl hydrolases family 2, TIM barrel domain. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ55906.1|GH2	0.0	1	879	1	858
EAA35570.1|GH2	0.0	1	879	1	854
UQC87618.1|GH2	0.0	4	880	28	877
AEO69937.1|GH2	0.0	1	879	1	851
AFJ59925.1|GH2|3.2.1.25	0.0	1	879	1	855

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	2.47e-140	4	688	23	666	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	9.89e-121	6	860	7	814	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	1.04e-120	6	860	9	816	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	1.06e-120	6	860	9	816	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	2.77e-120	6	860	7	814	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	1	879	1	855	Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1
sp|A1D911|MANBB_NEOFI	7.85e-293	8	868	7	834	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|A1CGA8|MANBB_ASPCL	1.58e-292	8	868	7	834	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
sp|Q4WAH4|MANBB_ASPFU	3.16e-292	8	868	7	834	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	4.48e-292	8	868	7	834	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
1.000068	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EJT77977.1.