CAZyme Information: PGTG_13091-t26_1-p1

Basic Information

• Species: Puccinia graminis
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia graminis
• CAZyme ID: PGTG_13091-t26_1-p1
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
594		66389.38	8.6772

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PgraminisCRL75-36-700-3	16309	418459	509	15800

• Gene Location: location=DS178302:7315-9775(-)

Full Sequence      

MMPTIIQASFLLILFIVGFSHQAHGSVKVSAQPPKKTDPVTSGPISLTDNHVSTYFGWST
WSLQAYKGKGYGYDWLTETNIKAHADILSKEFSHLGYTRINLDSGWQDAQLDKYGRTVLN
HTTFPGGIDHLSAYLAQKKLKLGLYYLPGIDSRAVNSKSVVMNTKYTADQIIQCPNKDAL
GCNRNTVNAFNAGMALNYSHPGAQMYINSIVEGLYSWGVSFVKLDGIVPGSSVDPPEYWK
YNVTADLMAWRRAIDELYEQKWQKQGRERIWLGASWKIPTNAGSTMEKYMNSFRVEQDIE
AYSETQMTTFDRVIRNAKTAALWSSVDANRKWKGARDLDSILISDMSLAECKTMVTIWAM
FGSIIYLGDDLTKLPEARKALVKNPEVLKLAILASTNQARLDGFDPSVQPAQTANLQSLN
QLEAKDTTAVHQKSAQECGELAEKRRIVVEYGTHQKVDNSDDFQKSCLKSRASEKLMSLQ
ALSAGEGVKPDQWSLQSWVLEQGQGDIYVAVINAGQQNSSDKPVKVDISLNKLQTLQKSP
RIKQMTGMRYSVRDLWNQKDLSSISFQDKIDSTLETHGSILLKFSPIQTPTTSQ

Enzyme Prediction     

No EC number prediction in PGTG_13091-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	214	400	7.8e-22	0.6899563318777293

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
269893	GH27	3.67e-61	57	398	4	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.
374582	Melibiase_2	1.31e-12	76	388	26	279	Alpha galactosidase A.
269892	GH36	2.34e-12	57	383	5	291	glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 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. GH36 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.
177874	PLN02229	2.51e-11	6	390	2	322	alpha-galactosidase
166449	PLN02808	4.88e-11	57	401	35	297	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCM93998.1|GH27	5.88e-55	55	388	35	354
BCL77684.1|CBM35|GH27	2.70e-53	44	400	46	388
UOZ10267.1|CBM35|GH27	1.10e-47	55	417	42	381
UKS28775.1|GH27	2.37e-47	55	419	47	379
QIZ00458.1|CBM35|GH27	5.69e-47	34	388	40	384

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NX0_A	9.83e-17	57	388	28	351	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	9.69e-16	57	388	28	351	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]
1UAS_A	1.34e-10	57	388	12	267	Chain A, alpha-galactosidase [Oryza sativa]
3A21_A	2.35e-09	53	388	11	289	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]
3A5V_A	4.76e-09	52	388	7	291	Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q92451|AGAL3_HYPJE	7.55e-18	57	316	186	433	Alpha-galactosidase 3 OS=Hypocrea jecorina OX=51453 GN=agl3 PE=1 SV=1
sp|C8VJZ7|AGAL8_EMENI	1.09e-14	57	391	84	407	Putative alpha-galactosidase 8 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=agl8 PE=5 SV=2
sp|Q8RX86|AGAL2_ARATH	1.97e-10	52	388	38	298	Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
sp|Q9FXT4|AGAL_ORYSJ	8.84e-10	57	388	67	322	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
sp|Q8VXZ7|AGAL3_ARATH	8.97e-09	57	219	76	229	Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000215	0.999781	CS pos: 25-26. Pr: 0.9732

TMHMM  Annotations     

There is no transmembrane helices in PGTG_13091-t26_1-p1.