CAZyme Information: PTTG_12051-t43_1-p1

Basic Information

• Species: Puccinia triticina
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
• CAZyme ID: PTTG_12051-t43_1-p1
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
603		69634.26	5.7471

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ptriticina1-1BBBDRace1	15692	630390	814	14878

• Gene Location: location=ADAS02000021.1:333707-336091(+)

Full Sequence      

MQVRLAVLSSLFLITTNSQGTIQQQLVLDPNHHQQHQQELSAFDRPPGTYLGWSSWSLQA
YRGEGYGFYWLTERNVKAQADILSKEFSPFGYDRINLDSGWQDAELDQYGRTILNTRTFP
SGIHHLQSYLARRNLKLGLYYLPGIDSRAVENQHPVMNTEYTADQIIQCPVIHHPLDSKR
RTKCHRPMANAFNAGYSLNYSHPGSQMYINSVVDGLYSWNVSFVKLDALVPGSSFDPEDY
PKCDTRADLAAWRRAIDSRYEEEWQYAGRERIWLVASWAIPTIEGPTMDLNADSWRVEQD
IEAYGERMTTFDRVIRNIKTAALWTSVEENRAWRGLIDLDSLLVSDMTYEESQSTVTLWA
VLGSPFYLGDDLTRLPESRKALVQNAEVLEVARLASWNPARLERFNQTRLEESRTMWQGD
RNQVNIEECERLVEKRRMVVELSLHQKVDPVHDLRQCLKTQINQSRSLPINPPRAYSRPD
TQENSEWSLQFWVLEHHDGVLFLAIVNAGGQNPFDMPVEVEIQLSELEKFQGTLQSMRKN
DNGQQGEERWYLVRDLWRRETLGVVSFQGKIKLRLAVHASVLFKFAPIGSDHSQYPLMSD
DSL

Enzyme Prediction     

No EC number prediction in PTTG_12051-t43_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	216	419	1.3e-25	0.74235807860262

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
269893	GH27	5.13e-67	46	391	1	268	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	1.29e-15	71	391	26	281	Alpha galactosidase A.
178770	PLN03231	1.73e-15	52	391	4	345	putative alpha-galactosidase; Provisional
166449	PLN02808	3.49e-15	51	391	34	292	alpha-galactosidase
177874	PLN02229	5.62e-14	51	391	65	322	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCM93998.1|GH27	2.51e-58	44	391	32	356
BCL77684.1|CBM35|GH27	3.34e-54	50	401	57	388
SDS59418.1|CBM35|GH27	5.88e-53	50	401	69	399
QNE35833.1|GH27	1.73e-52	50	391	103	416
QSF46401.1|GH27	2.63e-51	50	391	44	357

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NX0_A	1.02e-18	51	391	27	353	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	1.02e-17	51	391	27	353	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	1.14e-12	40	391	7	340	Chain A, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
1UAS_A	1.83e-10	51	391	11	269	Chain A, alpha-galactosidase [Oryza sativa]
1R46_A	1.58e-09	71	391	33	288	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	1.09e-18	52	305	186	417	Alpha-galactosidase 3 OS=Hypocrea jecorina OX=51453 GN=agl3 PE=1 SV=1
sp|C8VJZ7|AGAL8_EMENI	1.02e-12	52	399	84	414	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|Q8VXZ7|AGAL3_ARATH	1.09e-12	51	391	75	332	Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1
sp|Q8RX86|AGAL2_ARATH	1.57e-12	51	391	42	300	Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
sp|P14749|AGAL_CYATE	1.67e-11	51	391	58	316	Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000294	0.999649	CS pos: 18-19. Pr: 0.9805

TMHMM  Annotations     

There is no transmembrane helices in PTTG_12051-t43_1-p1.