CAZyme Information: P170DRAFT_443786-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_443786-t37_1-p1
• CAZy Family: GH43
• CAZyme Description: beta-mannosidase B

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
844	MSFO01000002|CGC29	96268.11	5.1469

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsteyniiIBT23096	13430	1392250	235	13195

• Gene Location: location=MSFO01000002:695677-698395(-)

Full Sequence      

MAAYSQHSLSTGWSFKDSEDASAEAWLPVPVVPSVVHQDLQANDKLKNPYVGFNELDARW
VNDKSWSYRNVFQKPSVPDGSSVVLAFDGLDTFATVKLDGKVILESNNMFLAHRVDVTKA
LEAEGDHVLEIDFDCAMLRARKLKEQDPKHNWASFNGDPARMAVRKAQYHWGWDWGPLLN
TAGIWREVRLEVYSARVEDLWTELKLASNHESAQISAFAQFEGVDSDSSYNVTFTLSLDG
QEVAREVTQPKDRYADVTFDVKQPSLWWPNGYGDPTLYDISVSLEKGQDEVHRASKKIGI
RTAEVIQRPDKHGKSFFFRINGVDVFCGGSCWIPADNLLPSISAERYRKWIELMVAGRQV
MIRVWGGGCYEDDSFYQACDELGVLVWQDFMFGCGNYPTWPDLLESVEQEAFYNVRRLRH
HPSIVIWVGNNEDYQVQEQAGLVYNYEDKNPENWLKTDFPARYIYEKLLPSVVEKLTPSI
FYHPGSPWGDGKTTSDPTVGDMHQWNVWHGTQEKYQIFDTLGGRFNSEFGMEAFPHLSTI
DYFVENEKDKYPQSHVLDFHNKADGHERRIATYLVENLRTATDLETYIYLTQVVQAETMM
FGYRGWRRQWGDERHCGGALLWQLNDCWPTISWAIVDYFLRPKPAFYAVARVLNPIAVGV
RREHHDWSVTHAQPPKTSKFELWIASNLQKEVSGKVELRFLSVNSGLEVRESIVHDNVKI
VPNGTTNIADGVIDHTEYPEPHVLAARLWVDGSVTARDVDWPQPFKYLDLSDRGLEVTKG
SGSATEQTLKITTKKPVKCLVFEERDGVRVSDSAMDIVPGDEQVVTIKGLGENDAPLKYK
FLGQ

Enzyme Prediction     

EC	3.2.1.25:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	5	728	1.8e-100	0.6888297872340425

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225789	LacZ	3.21e-85	5	658	11	634	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
407658	Mannosidase_ig	3.84e-15	678	767	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	1.29e-11	195	301	1	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
236548	lacZ	1.36e-04	183	305	208	338	beta-galactosidase.
397119	Glyco_hydro_2_C	0.010	375	434	64	137	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
UDD65874.1|GH2	0.0	1	844	1	844
QRD92384.1|GH2	0.0	1	844	1	844
QMW36571.1|GH2	0.0	1	844	1	833
QMW48626.1|GH2	0.0	1	844	1	833
BAE66106.1|GH2	0.0	1	844	1	849

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	2.07e-147	1	697	21	684	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	1.61e-131	9	827	11	816	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	1.69e-131	9	827	13	818	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	1.73e-131	9	827	13	818	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	4.54e-131	9	827	11	816	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|Q0CCA0|MANBB_ASPTN	0.0	1	844	1	843	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
sp|Q2TXB7|MANBB_ASPOR	0.0	1	844	1	844	Beta-mannosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=mndB PE=3 SV=3
sp|B0YBU9|MANBB_ASPFC	0.0	1	844	1	845	Beta-mannosidase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=mndB PE=3 SV=1
sp|A1CGA8|MANBB_ASPCL	0.0	1	844	1	845	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|B8NW36|MANBB_ASPFN	0.0	1	844	1	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000061	0.000000

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_443786-t37_1-p1.