CAZyme Information: CCE27857.1

Basic Information

• Species: Claviceps purpurea
• Lineage: Ascomycota; Sordariomycetes; ; Clavicipitaceae; Claviceps; Claviceps purpurea
• CAZyme ID: CCE27857.1
• CAZy Family: CE9
• CAZyme Description: Non-reducing end alpha-L-arabinofuranosidase [Source:UniProtKB/TrEMBL;Acc:M1VUJ0]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
342	CAGA01000006|CGC1	38453.98	7.8149

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Cpurpurea20.1	8979	1111077	156	8823

• Gene Location: location=CAGA01000006:225454-226482(+)

Full Sequence      

MKFLSLAWVGAAAAGLISHHHHGLSNRSSLPSKFSWTSTQPLIYPKNDGRNLKGIKDPSV
IFHEGKYHVFASTAQKAGYNLVYLSFTDWDQAQESTFHYLDQTPIGKGYRAAPQIFRIEE
QGLWYLVYQGRGATYSTNKDINDPSGWSAPKTFYPSIPSKIQSGMGHGQWVDMWVICDST
NCFMFSSDDNGHLWRAQTKLADFPSGFSQPVIALQESNVWKLYEASNVYNVGGAYLLIVE
AAGNDGNRYFRSWTAKTLDAQWTSLANTEQNPFIRSNNVKFGDGKAWTNNFSHGEVVRTN
VDQTMTIDPCKMQYLYQGRDTKSTGGYDDLPWKLALLTQNSC

Enzyme Prediction     

EC	3.2.1.55:25	3.2.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH62	29	311	5e-103	0.9928057553956835

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350101	GH62	5.83e-155	30	339	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	5.08e-58	29	310	2	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	1.31e-11	56	299	1	239	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.
350097	GH43_Bt3655-like	0.004	35	153	124	236	Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655. This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. 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. 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 GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 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.
350106	GH117	0.006	32	142	4	128	Glycosyl hydrolase family 117 (GH117). This glycoside hydrolase 117 (GH117) family includes alpha-1,3-L-neoagarooligosaccharide hydrolase (EC 3.2.1.-); alpha-1,3-L-neoagarobiase/neoagarobiose hydrolase (NABH, EC 3.2.1.-). In the agarolytic pathway, in order to metabolize agar, NABH is an essential enzyme because it converts alpha-neoagarobiose (O-3,6-anhydro-alpha-l-galactopyranosyl-(1,3)-d-galactose) into fermentable monosaccharides (d-galactose and 3,6-anhydro-l-galactose). Thus, these enzymes have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate. This family includes Zobellia galactanivorans enzymes, Zg4663 and Zg3615 (also known as ZgAhgA and ZgAhgB, respectively) that have been shown to have similar activity on unsubstituted agarose oligosaccharides while Zg3597 has been shown to be inactive, possibly due to differences in dimerization conformation, active-site structure and function. GH117 shares distant sequence similarity with families GH43 and GH32. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPH02528.1|GH62	2.01e-152	1	339	1	335
ACQ05660.1|GH62	4.70e-151	29	341	58	369
ANC68285.1|CBM1|GH62	3.08e-150	29	341	82	393
AQQ75323.1|CBM2|GH62	2.38e-148	29	341	177	491
UPK96217.1|GH62	1.15e-147	2	341	5	344

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5B6S_A	1.63e-146	30	341	1	313	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	4.38e-135	24	341	14	334	Chain A, GH62 arabinofuranosidase [Podospora anserina],4N4B_A Chain A, GH62 arabinofuranosidase [Podospora anserina]
4PVI_A	6.95e-125	23	339	13	342	Crystal structure of GH62 hydrolase in complex with xylotriose [Mycothermus thermophilus]
4PVA_A	4.59e-123	23	339	13	342	Crystal structure of GH62 hydrolase from thermophilic fungus Scytalidium thermophilum [Mycothermus thermophilus]
6F1J_A	2.02e-66	29	338	27	323	Structure of a Talaromyces pinophilus GH62 Arabinofuranosidase in complex with AraDNJ at 1.25A resolution [Talaromyces pinophilus],6F1J_B Structure of a Talaromyces pinophilus GH62 Arabinofuranosidase in complex with AraDNJ at 1.25A resolution [Talaromyces pinophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P23031|XYNC_CELJU	8.28e-68	25	337	318	615	Alpha-L-arabinofuranosidase C OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=xynC PE=1 SV=2
sp|Q0C8B3|AXHA_ASPTN	8.44e-65	23	338	21	323	Probable alpha-L-arabinofuranosidase axhA OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=axhA PE=3 SV=1
sp|Q5B9Z8|AXHA1_EMENI	8.69e-65	6	338	12	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|Q2U7D2|AXHA_ASPOR	3.54e-64	6	338	18	325	Probable alpha-L-arabinofuranosidase axhA OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=axhA PE=3 SV=1
sp|P79021|AXHA_ASPTU	1.11e-63	27	338	27	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
0.412814	0.587178	CS pos: 27-28. Pr: 0.3159

TMHMM  Annotations     

There is no transmembrane helices in CCE27857.1.