CAZyme Information: KIW16445.1

Basic Information

• Species: Exophiala spinifera
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala spinifera
• CAZyme ID: KIW16445.1
• CAZy Family: GH43
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
838	KN847495|CGC16	95588.39	5.7062

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EspiniferaCBS89968	12110	N/A	61	12049

• Gene Location: location=KN847495:3561089-3563605(+)

Full Sequence      

MKNYHFESRPVARPETVVSGANYRFTVLTDRLIRYEWSEDGQFEDRASTFAVNRDLSSKE
TKQNKTETDEEEEGAAAAVVVGTPKFQVVDHGEDGLEIINEYFHVSYDKKRFSPSGLLCT
FAAKITLWGSQWRYNDDVGASQGFNLGGTARTLDGCDGRCDMGYGVLSRDGYAAVDDSKS
MLFDGHGFVAGRRAGDRIDGYLFCHGLDYKGAMRDFYAVSGKQPLLPRWALGNWWSRYYR
YRQDEYVGLMDRFKDEGVPMSVAVVDMDWHLVNDERVPHAGWTGYTWDDKLFPDPGQFGR
EMHSRNLKITLNDHPHHGIHHHEDAYLEMAEFLGLDTSRHKNPILFDPTSPKFMQAYLDI
LHRKLEDVACDFWWIDWQQGSFTKVPGIDPLWLLNHFHFLDNARGGKQRPIIFSRYAGPG
SHRYPVGFSGDTVTTWASLEFQPEFTATASNIGYGWWSHDIGGHYGGTRDDELVTRWVQF
GVFSPVMRLHSSNSRWSSKEPWLYRKESEAIIVDFMRLRHRLIPYLYTRNVLAGTEEGLP
LVQPMYWLFPERDEAYSVPNQYFFGPELIVAPIVTPRDKRTNQAKVKVWLPPMHRHVDIF
TGTVYDGDRELNMYRPLEGMPVLAHEGSIVPLDANPVPGNGGLNPDHFEVLVVIGRDGQA
SVLEDPADDSDQVKKESPSTGERGSLIQYHQDEGDLVAHVTGRTWTFRFLAVTDVPKGFK
VCIDGDDRTGDAKVEIQKFPHTPSMLVRVPYVSDREKYAITVSLGPDPQLSVIDHRDRIE
RLLLDYQTEFDLKDKLWSIVDDRKSSINVKIGKLMSLSVDERLTEPVAELLLSDARGM

Enzyme Prediction     

No EC number prediction in KIW16445.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH31	201	630	5e-124	0.9976580796252927

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
269881	GH31_u1	3.79e-167	220	526	1	304	glycosyl hydrolase family 31 (GH31); uncharacterized subgroup. This family represents an uncharacterized GH31 enzyme subgroup found in bacteria and eukaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein.
395838	Glyco_hydro_31	2.33e-110	201	630	1	442	Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
224418	YicI	3.86e-108	163	665	202	704	Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
269876	GH31	4.68e-69	221	515	1	264	glycosyl hydrolase family 31 (GH31). GH31 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. In most cases, the pyranose moiety recognized in subsite -1 of the substrate binding site is an alpha-D-glucose, though some GH31 family members show a preference for alpha-D-xylose. Several GH31 enzymes can accommodate both glucose and xylose and different levels of discrimination between the two have been observed. Most characterized GH31 enzymes are alpha-glucosidases. In mammals, GH31 members with alpha-glucosidase activity are implicated in at least three distinct biological processes. The lysosomal acid alpha-glucosidase (GAA) is essential for glycogen degradation and a deficiency or malfunction of this enzyme causes glycogen storage disease II, also known as Pompe disease. In the endoplasmic reticulum, alpha-glucosidase II catalyzes the second step in the N-linked oligosaccharide processing pathway that constitutes part of the quality control system for glycoprotein folding and maturation. The intestinal enzymes sucrase-isomaltase (SI) and maltase-glucoamylase (MGAM) play key roles in the final stage of carbohydrate digestion, making alpha-glucosidase inhibitors useful in the treatment of type 2 diabetes. GH31 alpha-glycosidases are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
269877	GH31_xylosidase_XylS	2.46e-44	221	519	1	322	xylosidase XylS-like. XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in prokaryotes, eukaryotes, and archaea, that catalyzes the release of alpha-xylose from the non-reducing terminal side of the alpha-xyloside substrate. XylS has been characterized in Sulfolobus solfataricus where it hydrolyzes isoprimeverose, the p-nitrophenyl-beta derivative of isoprimeverose, and xyloglucan oligosaccharides, and has transxylosidic activity. All GH31 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. The XylS family corresponds to subgroup 3 in the Ernst et al classification of GH31 enzymes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UDD62125.1|GH31	0.0	1	836	1	800
QMW42444.1|GH31	0.0	1	836	1	800
QRD86856.1|GH31	0.0	1	836	1	800
QMW30372.1|GH31	0.0	1	836	1	800
BAE59606.1|GH31	0.0	1	836	223	1022

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7WJ9_A	5.84e-191	24	665	41	644	Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_B Chain B, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_C Chain C, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_D Chain D, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_E Chain E, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJ9_F Chain F, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJA_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJB_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_B Chain B, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_C Chain C, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_D Chain D, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_E Chain E, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WLG_F Chain F, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363]
7WJC_A	9.24e-190	24	665	41	644	Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJD_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJE_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363],7WJF_A Chain A, Alpha-xylosidase [Lactococcus lactis subsp. cremoris MG1363]
7KMP_A	1.04e-41	166	665	382	899	Chain A, Alpha-xylosidase [Xanthomonas citri pv. citri str. 306],7KNC_A Chain A, Alpha-xylosidase [Xanthomonas citri pv. citri str. 306]
2F2H_A	1.92e-37	201	673	239	711	Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_B Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_C Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_D Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_E Structure of the YicI thiosugar Michaelis complex [Escherichia coli],2F2H_F Structure of the YicI thiosugar Michaelis complex [Escherichia coli]
1XSI_A	1.97e-37	201	673	239	711	Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_B Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_C Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_D Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_E Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSI_F Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_A Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_B Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_C Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_D Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_E Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSJ_F Structure of a Family 31 alpha glycosidase [Escherichia coli],1XSK_A Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_B Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_C Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_D Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_E Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli],1XSK_F Structure of a Family 31 alpha glycosidase glycosyl-enzyme intermediate [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9P999|XYLS_SACS2	9.91e-47	166	665	155	656	Alpha-xylosidase OS=Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OX=273057 GN=xylS PE=1 SV=1
sp|Q5AW25|AGDD_EMENI	3.17e-43	201	652	257	717	Alpha-xylosidase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agdD PE=1 SV=1
sp|Q9F234|AGL2_BACTQ	1.94e-38	195	728	227	771	Alpha-glucosidase 2 OS=Bacillus thermoamyloliquefaciens OX=1425 PE=3 SV=1
sp|P31434|XYLS_ECOLI	9.85e-37	201	673	239	711	Alpha-xylosidase OS=Escherichia coli (strain K12) OX=83333 GN=yicI PE=1 SV=2
sp|B3PEE6|OL4AG_CELJU	2.10e-36	201	631	234	673	Oligosaccharide 4-alpha-D-glucosyltransferase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=agd31B PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000054	0.000001

TMHMM  Annotations     

There is no transmembrane helices in KIW16445.1.