CAZyme Information: PHYBL_189538T0-p1

Basic Information

• Species: Phycomyces blakesleeanus
• Lineage: Mucoromycota; Mucoromycetes; ; Phycomycetaceae; Phycomyces; Phycomyces blakesleeanus
• CAZyme ID: PHYBL_189538T0-p1
• CAZy Family: GT2
• CAZyme Description: Alpha-D-galactosidase (melibiase)

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
461		52027.49	6.5761

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PblakesleeanusNRRL1555	16528	763407	0	16528

• Gene Location: location=PblaNRRL1555-_SC43:86608-88174(+)

Full Sequence      

MGALAGPDRKDINIEPGCKPDWACKPMLGFSTWSTQILDDVPGYGGRTESPWFNETNIKE
ISNVMRQKMPDYEYINLDSGWSQECDENGRWMFRSELFPNGLKALSSHLATNGHKLGLYM
LPGIRKDAADANLLVKGTSHRLGDLVTMKRQGNGFKDTTYMPDVHNEVVQAYYDSIADLF
AEWGVSYVKVDGCGPGGGDQMYPYQSPDNRACLYMLATSFKQRNIWMELSWYLDHSYADE
WAYIANGARIFIDIESYSTKTMTSSFRVFQRITQASRWADKVVVGKKYGFFLDLDVVVVG
MTVDGNCIDGLDNDDIRLSYISFWALLSSVFCIGADPRKIPEKYLRMLCHPGIIAIHQSG
IMARPIQSGNVWTNRKQIWWKKMENGKICVGLFNAHVYMLILGMNQGFVLNLTDVGITAA
DIEDVWTGQNLGTHKDTYKVYLRPGQCQILMLTPKTSSPLS

Enzyme Prediction     

No EC number prediction in PHYBL_189538T0-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	176	432	5.1e-36	0.9475982532751092

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
269893	GH27	9.87e-58	26	358	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	6.18e-18	54	455	47	386	alpha-galactosidase
177874	PLN02229	2.44e-12	54	458	78	423	alpha-galactosidase
178295	PLN02692	1.87e-11	72	434	92	389	alpha-galactosidase
374582	Melibiase_2	2.23e-11	58	358	31	283	Alpha galactosidase A.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS03372.1|GH27	4.02e-234	19	454	27	464
CDS10147.1|GH27	1.40e-210	25	453	11	442
QSF46401.1|GH27	1.19e-61	13	455	30	448
CCW35282.1|GH27	4.40e-60	23	455	26	438
AYB44719.1|GH27	7.15e-59	13	453	31	444

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NX0_A	6.45e-20	22	460	21	448	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]
1UAS_A	6.24e-19	26	454	9	361	Chain A, alpha-galactosidase [Oryza sativa]
4NXK_A	6.77e-19	22	460	21	448	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]
3A21_A	3.51e-16	59	458	33	389	Crystal Structure of Streptomyces avermitilis beta-L-Arabinopyranosidase [Streptomyces avermitilis],3A21_B Crystal Structure of Streptomyces avermitilis beta-L-Arabinopyranosidase [Streptomyces avermitilis],3A22_A Crystal Structure of beta-L-Arabinopyranosidase complexed with L-arabinose [Streptomyces avermitilis],3A22_B Crystal Structure of beta-L-Arabinopyranosidase complexed with L-arabinose [Streptomyces avermitilis],3A23_A Crystal Structure of beta-L-Arabinopyranosidase complexed with D-galactose [Streptomyces avermitilis],3A23_B Crystal Structure of beta-L-Arabinopyranosidase complexed with D-galactose [Streptomyces avermitilis]
6F4C_B	3.38e-15	26	455	9	363	Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q55B10|AGAL_DICDI	2.98e-21	23	454	25	383	Probable alpha-galactosidase OS=Dictyostelium discoideum OX=44689 GN=melA PE=3 SV=1
sp|Q9FXT4|AGAL_ORYSJ	5.15e-18	26	454	64	416	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
sp|Q92451|AGAL3_HYPJE	1.43e-17	29	452	186	620	Alpha-galactosidase 3 OS=Hypocrea jecorina OX=51453 GN=agl3 PE=1 SV=1
sp|Q8RX86|AGAL2_ARATH	1.13e-16	23	453	37	392	Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
sp|Q8VXZ7|AGAL3_ARATH	1.99e-15	26	458	73	433	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
1.000035	0.000003

TMHMM  Annotations     

There is no transmembrane helices in PHYBL_189538T0-p1.