CAZyme Information: P170DRAFT_455548-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_455548-t37_1-p1
• CAZy Family: GH67
• CAZyme Description: glycoside hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
850		97425.50	5.5884

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=MSFO01000003:4455661-4458391(+)

Full Sequence      

MSEFRSKELSDDWKLRDATDTNTETWYTVTAVPTVVHLDLLQNGIIPDPFIGLNEEKAQW
VAERDWIYQTTFETPPGDPKTRHSVAFDGLDTFATVKLNGNVILRSDNMFIPHRVDITDI
LASSPSTTNTLEILFESALLRAREVVKSHPEHRHIAHQTEVGRLGARKAAYHWGWDWGPI
LVTAGPWRPVTLESYADRIDDLWIESTVADDLRSCAGKIRVRTEGRGADRVHIALWHEGK
VAIEADVEVDPQGEANVSFCIESPALWFPHGYGPQSRYEIRAELFLQDDLLHAKSKRTGF
RRAELIQEKDEHGQSFYFRINNVDVFASGSCWIPGDSFLPQITDAKYRKWLTLIVEGNQN
MIRIWGGGIFEPEVFYETCDELGIMVFQDFLFACASYPTYPEYLQSVEKEARANVQLLRH
HPSIVIYAGNNEDYQIQQKYNLTYDYDGDKDPESWLKSSFPARYIYEYLLPKVVEEESPG
MAYHPSSPWGGGRHTTDPTIGDIHQWDVWHGTMEPYQKLSSMGGRFNSEFGMEAFPHMYT
IDSFVDDPEERYHQSLTMDFHNKASGHERRLGAYILENFNVKQDLKAYIHLSQIAQSETM
TFAYRSWRREWGRKRRCGGVLVWQLNDCWPTISWAIVDYFLVKKPAFYAIARASQPLAIG
VSRRHKEWTSGHARSPSSVEFDVWTASSKAERVHAVVTVRYISVETGHDFKPASVHTVEV
VPNGTTEILGDRVDLNRNSTEKEEVQPFVIFATLSVDGAIVSRDFDWPQPLKYLKFRERD
VKVEFLKEESSVRVAVSKPTKGLVFEERPGIWFGDNGIDLVPGDERIIPVKGIAGYDSIP
RWTYIGDNRF

Enzyme Prediction     

EC	3.2.1.25:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	5	728	2.6e-92	0.6888297872340425

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225789	LacZ	7.06e-75	1	664	9	639	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
395572	Glyco_hydro_2	5.50e-08	198	301	2	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
407658	Mannosidase_ig	9.09e-08	680	773	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.
397119	Glyco_hydro_2_C	0.005	373	434	62	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
BCS19382.1|GH2	0.0	1	849	1	849
QMW26140.1|GH2	0.0	1	849	1	842
QRD87794.1|GH2	0.0	1	849	4	845
QMW38223.1|GH2	0.0	1	849	1	842
BAE55770.1|GH2	0.0	1	849	1	842

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	1.42e-141	1	665	21	664	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	1.10e-116	23	840	22	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	1.15e-116	23	840	24	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	1.18e-116	23	840	24	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	3.08e-116	23	840	22	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|Q2TXB7|MANBB_ASPOR	0.0	1	846	1	843	Beta-mannosidase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=mndB PE=3 SV=3
sp|Q5B7W2|MANBB_EMENI	0.0	1	846	1	842	Beta-mannosidase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=mndB PE=1 SV=2
sp|Q4WAH4|MANBB_ASPFU	0.0	1	846	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
sp|B0YBU9|MANBB_ASPFC	0.0	1	846	1	844	Beta-mannosidase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=mndB PE=3 SV=1
sp|Q0CCA0|MANBB_ASPTN	0.0	1	846	1	842	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000045	0.000000

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_455548-t37_1-p1.