CAZyme Information: OJD17283.1

Basic Information

• Species: Emergomyces pasteurianus
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Emergomyces; Emergomyces pasteurianus
• CAZyme ID: OJD17283.1
• CAZy Family: GT17
• CAZyme Description: Beta-mannosidase A [Source:UniProtKB/TrEMBL;Acc:A0A1J9QAM7]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
860		98256.01	5.7059

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EpasteurianusEp9510	9078	1447872	128	8950

• Gene Location: location=LGRN01000073:53347-56111(-)

Full Sequence      

MAERSVIPLKNGWVFKQADDEKADFLPVSQFPTNVHLDLMHHGLIPDPFIGKNELDVQWV
GEKSWEYKTSFDAPPLKDGSKAVLAFDGLDTHATVLLNDTKILETDNMFIPERVDVTELL
RKSRGSNVLKIIFDSTYLIGKKLKEQHPEHRWVCWNGDCSRLAVRKAQYHYGWDWGPTLM
TCGPWRGVNLEIYNARISDLHFRQNVDKSLKQAELVVTAEVEGDAKTVVFHISLGDEDKG
SEMIDIKDGIATVTFHVQDPQLWYPSTYGKQPLYRLSASLSSNGVKLDSISKRVGLRRAQ
LIQRKMDDAEGTSFFFEVNNIPVFCGGSDWIPADNFIPRISPQKYYDWVKLMVEGNQVMV
RVWGGGIFEEQAFYDACDELGLLVWQDFLFGCGNYPVFPSFLETVKREAIANVKILRHHP
SIVIWAGNNEDYQLAESEKLNWDPNDNDPDSWLKSEFPARYIYEKILVDVTKDLIPDTYY
HFGSPWGGKNTSDPTIGDIHQWNVWHGTQEKYQDYDKLSGRFVSEFGMQGFPSMKTIDGY
LAGGKTDPDRYPQSSTVDFHNKAAGHERRTALYLAENIQYNLEPFEQYIYSTQLIQAECL
ASAYRLWKRQWKGPGREYCAGVLVWQINDCWPVTSWAIVDYHLRPKHAFYTVKRELAPIT
IGLKRTSHTEYADKYTNAFYKTTHKIEMWASNLTVGQRSVGVMVKAWDVMTGRETYSEKL
HDRFVLEANRSTEIAEFEVPVHDKKRDSRDGEEANRTVVAAYLIENGEQVARYVNWPEPL
RYTHLQLPKKLQVTLSEDGKQVGLSAEVPVKGVAVYADEDEVVFEDNCVDLVPGETVYIG
VKGLAKGQGDKISVRYLGSS

Enzyme Prediction     

EC	3.2.1.25:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	3	748	9.3e-92	0.7047872340425532

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225789	LacZ	6.15e-77	1	653	7	627	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
395572	Glyco_hydro_2	1.45e-12	195	297	1	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
407658	Mannosidase_ig	7.59e-12	685	782	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.
236657	PRK10150	5.26e-07	67	324	69	293	beta-D-glucuronidase; Provisional
407625	Ig_mannosidase	4.03e-05	790	842	5	57	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
QSS71278.1|GH2	0.0	1	859	1	859
QSS62028.1|GH2	0.0	1	859	1	859
UQC87618.1|GH2	0.0	1	858	26	874
ATZ49691.1|GH2	0.0	1	858	24	877
CCD56258.2|GH2	0.0	1	858	1	854

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	5.57e-140	1	664	21	661	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	2.77e-123	6	857	8	834	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	2.91e-123	6	857	10	836	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	2.99e-123	6	857	10	836	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	7.80e-123	6	857	8	834	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	858	1	853	Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1
sp|A1D911|MANBB_NEOFI	6.14e-287	1	858	1	844	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|Q0CCA0|MANBB_ASPTN	8.12e-287	9	858	9	842	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
sp|A1CGA8|MANBB_ASPCL	1.61e-284	1	858	1	844	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	2.99e-282	1	858	1	844	Beta-mannosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=mndB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000058	0.000000

TMHMM  Annotations     

There is no transmembrane helices in OJD17283.1.