CAZyme Information: CDH57482.1

Basic Information

• Species: Lichtheimia corymbifera
• Lineage: Mucoromycota; Mucoromycetes; ; Lichtheimiaceae; Lichtheimia; Lichtheimia corymbifera
• CAZyme ID: CDH57482.1
• CAZy Family: GT2
• CAZyme Description: melibiase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
541	CBTN010000046|CGC1	61848.61	6.4991

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LcorymbiferaJMRCFSU9682	12379	1263082	97	12282

• Gene Location: location=CBTN010000046:200875-203325(-)

Full Sequence      

MNNRLYWIGQDGDDLTCSRELGRQTSMILVHCSVITCLLFQLTSDLAPSFSLLIAVNIPV
LLLGDCFGITKRKLMMAPPATSLSSSSPLSRDSKAYFDIDNKPEWARKPLLGFSTWSTQL
LDDVPGYGGKHTEPWFNESKIKAVSDAMKLRLPKYEYINLDSGWSETFDEYGRWTYRKDL
FPNGLRELSDHLRRNGHKLGLYMLPGIRKDAYEANTPILGTEYRLQDLVVDKKEGNGFKG
STYMPDNHLDIVQQYYDSIADAFAEWGVSFVKIDGCGPGGGDQFYPYQSPDTREDLKMMA
RAFKRYDIWLELSWFMDHTYANDWALLSNGARVFIDIESYSTRTMTSSHRVFQRFTQAAR
WVDYNVVGSDHGFYIDLDVVLVGMVVNGKCVDGLDNDDVRMSYISFWALVSSVFCIGADP
RMIPDKYLAMLNHSDILAIHQAGNMARPIGSGDVWQNRKQVWWKRMPDGRICCGLFNAHT
YMFMLGKSHEITLDLKEVGFTNSQQVKLFDIWEGKDIGVFTDNYRVRLRPGQCQMLFLTK
V

Enzyme Prediction     

No EC number prediction in CDH57482.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	258	517	5.2e-36	0.9475982532751092

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
269893	GH27	1.68e-61	109	441	1	270	glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 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. GH27 members 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.
166449	PLN02808	2.07e-19	109	539	32	384	alpha-galactosidase
178295	PLN02692	9.42e-16	109	541	56	411	alpha-galactosidase
407673	Melibiase_C	2.74e-13	460	538	5	74	Alpha galactosidase C-terminal beta sandwich domain. This domain is found at the C-terminus of alpha galactosidase enzymes.
177874	PLN02229	4.49e-12	106	517	60	395	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS03372.1|GH27	0.0	76	538	1	462
CDS10147.1|GH27	2.14e-206	107	539	10	442
AYB44719.1|GH27	1.85e-75	104	539	39	444
QSF46401.1|GH27	1.17e-72	104	539	38	446
QQZ58671.1|GH27	2.08e-68	106	524	37	429

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NX0_A	8.44e-30	104	539	20	441	Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_B Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_C Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_D Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_E Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_F Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_G Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NX0_H Crystal structure of Abp-WT, a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus]
4NXK_A	5.27e-29	104	539	20	441	Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_B Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_C Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_D Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_E Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_F Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_G Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NXK_H Crystal structure of Abp-D197A, a catalytic mutant of a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],4NZF_A Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_B Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_C Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_D Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_E Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_F Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_G Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus],4NZF_H Crystal structure of Abp-D197A (a GH27-b-L-arabinopyranosidase from Geobacillus stearothermophilus), in complex with arabinose [Geobacillus stearothermophilus]
3CC1_A	4.05e-19	106	539	9	430	Chain A, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
1UAS_A	6.96e-19	107	539	7	360	Chain A, alpha-galactosidase [Oryza sativa]
1R46_A	7.91e-12	106	456	6	310	Structure of human alpha-galactosidase [Homo sapiens],1R46_B Structure of human alpha-galactosidase [Homo sapiens],1R47_A Structure of human alpha-galactosidase [Homo sapiens],1R47_B Structure of human alpha-galactosidase [Homo sapiens],3GXN_A Crystal structure of apo alpha-galactosidase A at pH 4.5 [Homo sapiens],3GXN_B Crystal structure of apo alpha-galactosidase A at pH 4.5 [Homo sapiens],3GXP_A Crystal structure of acid-alpha-galactosidase A complexed with galactose at pH 4.5 [Homo sapiens],3GXP_B Crystal structure of acid-alpha-galactosidase A complexed with galactose at pH 4.5 [Homo sapiens],3GXT_A Crystal structure of alpha-galactosidase A at pH 4.5 complexed with 1-deoxygalactonijirimycin [Homo sapiens],3GXT_B Crystal structure of alpha-galactosidase A at pH 4.5 complexed with 1-deoxygalactonijirimycin [Homo sapiens],3HG2_A Human alpha-galactosidase catalytic mechanism 1. Empty active site [Homo sapiens],3HG2_B Human alpha-galactosidase catalytic mechanism 1. Empty active site [Homo sapiens],3HG4_A Human alpha-galactosidase catalytic mechanism 3. Covalent intermediate [Homo sapiens],3HG4_B Human alpha-galactosidase catalytic mechanism 3. Covalent intermediate [Homo sapiens],3HG5_A Human alpha-galactosidase catalytic mechanism 4. Product bound [Homo sapiens],3HG5_B Human alpha-galactosidase catalytic mechanism 4. Product bound [Homo sapiens],3S5Y_A Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3S5Y_B Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3S5Z_A Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3S5Z_B Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],4NXS_A Crystal structure of human alpha-galactosidase A in complex with 1-deoxygalactonojirimycin-pFPhT [Homo sapiens],4NXS_B Crystal structure of human alpha-galactosidase A in complex with 1-deoxygalactonojirimycin-pFPhT [Homo sapiens],6IBK_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfamidate ME763 [Homo sapiens],6IBK_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfamidate ME763 [Homo sapiens],6IBM_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfate ME776 [Homo sapiens],6IBM_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfate ME776 [Homo sapiens],6IBR_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol epoxide LWA481 [Homo sapiens],6IBR_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol epoxide LWA481 [Homo sapiens],6IBT_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol aziridine ME737 [Homo sapiens],6IBT_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol aziridine ME737 [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q92451|AGAL3_HYPJE	4.85e-22	112	540	186	622	Alpha-galactosidase 3 OS=Hypocrea jecorina OX=51453 GN=agl3 PE=1 SV=1
sp|Q9FXT4|AGAL_ORYSJ	5.94e-18	107	539	62	415	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
sp|Q55B10|AGAL_DICDI	4.72e-17	106	539	25	382	Probable alpha-galactosidase OS=Dictyostelium discoideum OX=44689 GN=melA PE=3 SV=1
sp|A2QEJ9|AGALB_ASPNC	1.28e-16	107	536	25	437	Probable alpha-galactosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=aglB PE=3 SV=1
sp|Q8VXZ7|AGAL3_ARATH	2.20e-16	92	539	56	428	Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000007	0.000008

TMHMM  Annotations     

There is no transmembrane helices in CDH57482.1.