CAZyme Information: PMAA_017530-t26_1-p1

Basic Information

• Species: Talaromyces marneffei
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces marneffei
• CAZyme ID: PMAA_017530-t26_1-p1
• CAZy Family: CBM50|CBM50
• CAZyme Description: alpha-L-arabinofuranosidase precursor, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
333	DS995899|CGC21	35448.59	6.4797

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmarneffeiATCC18224	10194	441960	145	10049

• Gene Location: location=DS995899:594438-595439(-)

Full Sequence      

MFSIASALFLALPVVSGLALPNDETLANSKRATCALPSRYSWTSTGSLANPASGLLALKD
FTHVPYNGQHLVYASDVNSASNYGSLSFALFSDWSSMAGATQHTMNTGAVAPNLFHFTPK
NIWVLAYEWCASPFCYRTSSDPTNANGWSSPQPLFSGSLSGGSAPIDPAIIGDSKNMYLF
FGADNGKIYRASMPIGNFPGNFGTSATVVLSDSTNNLFEAVQVYSVQGQNLYLMIVEAIG
ANGRYFRSFTATSLDGAWTPQATSESAPFAGKANSGATWTNDISSGDLIRSSADHTMPID
PCNLQFLYQGRAPNSGGTYNSLPYRPGLLTLKH

Enzyme Prediction     

EC	3.2.1.55:25	3.2.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH62	34	303	2.6e-121	0.9964028776978417

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
281639	Glyco_hydro_62	2.52e-148	34	303	1	272	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.
350101	GH62	3.53e-145	36	331	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.
350092	GH_F	4.91e-25	59	295	1	243	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX53721.1|GH62	6.23e-174	30	333	21	328
QGA12560.1|GH62	1.21e-168	105	333	1	229
UKZ84376.1|GH62	1.04e-167	31	333	26	327
AUG87704.1|GH62|3.2.1.55	1.24e-163	6	331	5	324
AIO06736.1|CBM1|GH62	8.53e-162	28	331	90	393

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F1J_A	4.30e-165	6	331	5	324	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]
6CC7_A	8.49e-159	24	332	10	318	Structure of Fungal GH62 from Thielavia terretris [Thermothielavioides terrestris NRRL 8126]
3WMY_A	7.21e-155	33	332	138	437	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)]
4O8N_A	1.74e-152	15	332	64	383	Crystal structure of SthAraf62A, a GH62 family alpha-L-arabinofuranosidase from Streptomyces thermoviolaceus, in the apoprotein form [Streptomyces thermoviolaceus],4O8O_A Crystal structure of SthAraf62A, a GH62 family alpha-L-arabinofuranosidase from Streptomyces thermoviolaceus, bound to alpha-L-arabinose [Streptomyces thermoviolaceus],4O8P_A Crystal structure of SthAraf62A, a GH62 family alpha-L-arabinofuranosidase from Streptomyces thermoviolaceus, bound to xylotetraose [Streptomyces thermoviolaceus]
5UBJ_A	3.97e-145	32	332	25	328	Structure of an alpha-L-arabinofuranosidase (GH62) from Aspergillus nidulans [Aspergillus nidulans FGSC A4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P96463|EABF_STRLI	3.93e-155	33	333	175	475	Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces lividans OX=1916 GN=abfB PE=1 SV=2
sp|O54161|EABF_STRCO	1.29e-153	33	332	175	474	Extracellular exo-alpha-L-arabinofuranosidase OS=Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) OX=100226 GN=abfB PE=1 SV=1
sp|Q5B9Z8|AXHA1_EMENI	1.49e-153	32	332	26	327	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	4.19e-151	26	332	20	327	Probable alpha-L-arabinofuranosidase axhA OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=axhA PE=3 SV=1
sp|Q9UVX6|AXHA_ASPSO	1.39e-149	26	332	20	327	Alpha-L-arabinofuranosidase axhA OS=Aspergillus sojae OX=41058 GN=axhA PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000386	0.999588	CS pos: 17-18. Pr: 0.9678

TMHMM  Annotations     

There is no transmembrane helices in PMAA_017530-t26_1-p1.