CAZyme Information: P174DRAFT_446675-t37_1-p1

Basic Information

• Species: Aspergillus novofumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus novofumigatus
• CAZyme ID: P174DRAFT_446675-t37_1-p1
• CAZy Family: GH35
• CAZyme Description: glycosyl hydrolase family 62 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
369		39898.52	7.6974

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnovofumigatusIBT16806	11729	1392255	197	11532

• Gene Location: location=MSZS01000001:296385-297625(-)

Full Sequence      

MRAIGATLLGLAVAVQAQQPLYAQCGGNGWTGSTQCVAGACCSSINAWYYQCLSGNCMPS
TTMTTTATRTTSTSTSGATGSLPTSFKWSSTNALVGPKNDGRNLAGIKDPSIIEVDGTYH
VFASTAQASGYNLVIPRCPQVFYFQPQQAWYLIFQNGNAAYSTNKDISNPAGWSAPKNFF
SSVPSIITQNIGNGYWVDMWVICDSSNCYLFSSDDNGHLYRSQTTLSNFPNGMGNTVIAL
SDSNPNNLFEASNVYRVGNQYLLIVEAIGSDGNRYFRSWTAPSLTGTWTGLANTEANPFA
RWNNVVFSGTSWTKSISHGEMVRSQVDQTMTISPCKLRYLYQGLSPTASGDYNSLPWKLA
LLTQTNSAC

Enzyme Prediction     

EC	3.2.1.55:25	3.2.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH62	138	336	6.1e-90	0.7086330935251799

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350101	GH62	1.40e-150	82	364	1	304	Glycosyl hydrolase family 62, characterized arabinofuranosidases. The glycosyl hydrolase family 62 (GH62) includes eukaryotic (mostly fungal) and prokaryotic enzymes which are characterized arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. These enzymes show significantly different substrate preference with rather low specific activity towards natural substrates and differ in catalytic efficiency. They do not act on xylose moieties in xylan that are adorned with an arabinose side chain at both O2 and O3 positions, nor do they display any non-specific arabinofuranosidase activity. The synergistic action in biomass degradation makes GH62 promising candidates for biotechnological improvements of biofuel production and in various biorefinery applications. These enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan.
281639	Glyco_hydro_62	3.56e-60	82	335	3	271	Glycosyl hydrolase family 62. Family of alpha -L-arabinofuranosidase (EC 3.2.1.55). This enzyme hydrolyzed aryl alpha-L-arabinofuranosides and cleaves arabinosyl side chains from arabinoxylan and arabinan.
350092	GH_F	2.71e-11	108	327	1	242	Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 enzymes, is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
395595	CBM_1	7.74e-11	21	49	1	29	Fungal cellulose binding domain.
197593	fCBD	2.39e-10	20	53	1	34	Fungal-type cellulose-binding domain. Small four-cysteine cellulose-binding domain of fungi

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANC68285.1|CBM1|GH62	2.94e-244	1	369	1	396
ACQ05660.1|GH62	1.45e-229	26	369	2	372
CCA70771.1|CBM1|GH62	4.48e-167	12	366	13	397
ACQ07729.1|GH62	7.99e-166	78	369	23	341
ANC68284.1|GH62	2.72e-164	78	369	14	332

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5B6S_A	9.58e-148	82	369	1	316	Chain A, Glycosyl hydrolase family 62 protein [Coprinopsis cinerea okayama7#130],5B6S_B Chain B, Glycosyl hydrolase family 62 protein [Coprinopsis cinerea okayama7#130],5B6T_A Chain A, Glycosyl hydrolase family 62 protein [Coprinopsis cinerea okayama7#130],5B6T_B Chain B, Glycosyl hydrolase family 62 protein [Coprinopsis cinerea okayama7#130]
4N2Z_A	3.66e-131	82	369	22	337	Chain A, GH62 arabinofuranosidase [Podospora anserina],4N4B_A Chain A, GH62 arabinofuranosidase [Podospora anserina]
4PVI_A	1.49e-113	84	364	22	342	Crystal structure of GH62 hydrolase in complex with xylotriose [Mycothermus thermophilus]
4PVA_A	5.56e-111	84	364	22	342	Crystal structure of GH62 hydrolase from thermophilic fungus Scytalidium thermophilum [Mycothermus thermophilus]
3WMY_A	9.63e-69	79	363	138	435	Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase [Streptomyces coelicolor A3(2)],3WMZ_A Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase ethylmercury derivative [Streptomyces coelicolor A3(2)],3WN0_A Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase in complex with L-arabinose [Streptomyces coelicolor A3(2)],3WN1_A Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase in complex with xylotriose [Streptomyces coelicolor A3(2)],3WN2_A Crystal Structure of Streptomyces coelicolor alpha-L-arabinofuranosidase in complex with xylohexaose [Streptomyces coelicolor A3(2)]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q5B9Z8|AXHA1_EMENI	2.63e-71	81	363	29	325	Probable alpha-L-arabinofuranosidase axhA-1 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=axhA-1 PE=3 SV=2
sp|P23031|XYNC_CELJU	3.61e-68	54	362	295	615	Alpha-L-arabinofuranosidase C OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=xynC PE=1 SV=2
sp|O54161|EABF_STRCO	1.25e-67	79	363	175	472	Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=abfB PE=1 SV=1
sp|P96463|EABF_STRLI	3.76e-66	79	363	175	472	Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces lividans OX=1916 GN=abfB PE=1 SV=2
sp|P79021|AXHA_ASPTU	5.21e-66	81	363	29	329	Probable alpha-L-arabinofuranosidase axhA OS=Aspergillus tubingensis OX=5068 GN=axhA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000362	0.999604	CS pos: 17-18. Pr: 0.9731

TMHMM  Annotations     

There is no transmembrane helices in P174DRAFT_446675-t37_1-p1.