CAZyme Information: KDQ26149.1

Basic Information

• Species: Pleurotus ostreatus
• Lineage: Basidiomycota; Agaricomycetes; ; Pleurotaceae; Pleurotus; Pleurotus ostreatus
• CAZyme ID: KDQ26149.1
• CAZy Family: CE16
• CAZyme Description: glycoside hydrolase family 2 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
907	KL198010|CGC5	103759.55	6.3679

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PostreatusPC15	12460	1137138	164	12296

• Gene Location: location=KL198010:2936569-2940137(+)

Full Sequence      

MLNTVLDKGWFWKQRQDSIAEVVKELAHGLPDDSHDVSRGSIIGGWQLAVAFPSEVHVEL
LRSQWIPHPFVAFNEHKVQWIGEVEWLYYCTFKGPRLEPGQCSELIFEGLDTVCDVYLNQ
SKIISADNMFRTYTYLLDGEGPATSSQQNTLLLHFKPAKKLAKAEEEKYGKVRAGSTNLG
DPSRVYLRKAQYDWRWDWGPELMTCGPYRSIRIETYLARIQEVQPCITVHFPESSSSTFV
ARVSVNAVVQGDFNKDYAIVVSLKHLNGRTIRTARQEIPHKTEKLKKVSLKGIVDWSLND
DNIRLWWPVGYGTQSLYSLQVDLTDEVIHQITKRIGFRSVSLVQEPLKEPDQYGTGSTFL
FEINRVRMFMGGSNWVPADNFLTTITPERYRAWLTLLVKGNQNMVRLWGGGVYEPDVFYD
ICDELGILVWQDFQFACGVYPAHDEFVENVRKEAEDNVRRLRHHPSIALFCGNNEDYQQV
LQWGGIDTLPARKIYEEVLPAVVSGLTEPPIPYHRGSPYGGKGWDTSDPTIGDVHQWNIW
GGKELPYQSYDELGGRFVSEFGIPSMPNMKTIESWMEGAAESDWHPQSIWMAQHTRAGSF
ERRFAILMNENFRMTSDFETFATSYAYQSWRRKWRGKGKEYTAGALIWQLNDCWPVTSWA
IVDYYLRPKPAYYTISRQLAEVAVGITRTVIQNRDHDRPRQFYEFGAIQSHGARIDIWGM
NSSLQLIDAELELYCVDLNSDWFHKETRGVHLLPNQSTELISMPCPGPPKASARKDADPY
KVPEWTSTSSVIVSARLINPSTGEVLARHADWPQPFKYLRIPDPKITVKVDAVKEELRVS
VDRPAKGVFFNIDGGGTESQEFGDGILWSDNALDMMPGENRIINVSGLRNRRIYVTYLGK
EKPSLVQ

Enzyme Prediction     

EC	3.2.1.25:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	42	726	1.2e-81	0.6382978723404256

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225789	LacZ	1.87e-65	51	675	33	626	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
407658	Mannosidase_ig	2.48e-14	715	818	3	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.
407625	Ig_mannosidase	1.10e-06	823	883	1	54	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
QRV98035.1|GH2	0.0	3	899	4	920
QRW12613.1|GH2	0.0	3	902	4	921
QRV83983.1|GH2	6.35e-314	3	902	4	899
QRW25365.1|GH2	2.14e-309	6	883	8	858
CCA67509.1|GH2	1.16e-289	6	902	8	859

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	7.99e-120	53	877	49	802	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	1.51e-105	53	903	31	828	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	1.57e-105	53	903	33	830	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	1.61e-105	53	903	33	830	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	4.16e-105	53	903	31	828	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	4.25e-196	52	899	31	853	Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1
sp|A1D911|MANBB_NEOFI	6.39e-186	33	889	17	832	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|B8NW36|MANBB_ASPFN	2.45e-185	46	900	26	844	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
sp|Q2TXB7|MANBB_ASPOR	4.87e-185	46	900	26	844	Beta-mannosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=mndB PE=3 SV=3
sp|A2QYN2|MANBB_ASPNC	6.87e-185	6	900	9	844	Beta-mannosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=mndB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000049	0.000000

TMHMM  Annotations     

There is no transmembrane helices in KDQ26149.1.