CAZyme Information: PHYSODRAFT_545197-t26_1-p1

Basic Information

• Species: Phytophthora sojae
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
• CAZyme ID: PHYSODRAFT_545197-t26_1-p1
• CAZy Family: GT71
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
754	JH159154|CGC19	81716.84	5.4274

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsojaeP6497	28142	1094619	1653	26489

• Gene Location: location=JH159154:3622191-3624512(+)

Full Sequence      

MAASTNSAYPAKDGWFQFDAASATSLEFVFNDGVGIVWDNNNNANYKVSAAGSYSVVSKV
SGFKTGDLPYIHFNAGSGWTTVSGYAMTASTYAGKFSAANGWYQYDISSTSSVEIAFNDG
NGVWDSNLNANYVRSSPGAYAFVNQNTQTPTSAPSVQGYVNGPGYAVTSTSESAGVLTIN
LQVNSAATATSYGSDLSALVVTVAKTESDSVRVKIVDKNNKRWEVPKSIFTAGTLGADST
ATAAAADPLYTFNYTQNPFTFQVTRKSDGYTLFDSSGISLVVKDQYLQASTVLGSDLSVY
GIGESTRENFKMASGDKQTLWARDQGSASANVNTYGSHPFFLGVNSAGQAHGVLLLNSNG
MDVTMDSGHLVYQTIGGVLDFNIVVGPTPANVVSQYTKLIGRPKLMPYWSYGFHQCRWGY
GSVDALRTVVSKYASNKLPLDVIWSDIDYMRSYHDFTLDPTNFPQAKMAAFMDEIHAAGQ
KFVPIIDPGIPDDTNDYAYTKGLSMDIFIKDTSGKPYLGQVWPGPTVFPDFFHPNAKSYW
GEQIQLMYKNFAFDGLWIDMNELANFCPGTTCVRQSGVTCPNTGSINAITTCCLSCSGDG
NKYDNPPFKINNVNSHDAIYNKGISTSALQYGNIRQYDAHNLYGITESIVTNSVQEELAN
KRSFVLSRSTFPGSGVHVAHWTGDNAATWNDLRWSIPTILKFGLFGIPMVGADICGFSGA
SNMELCARWTALGSFYPFSRNHNNLEAPSQETYV

Enzyme Prediction     

EC	3.2.1.20:35	3.2.1.177:14

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH31	383	753	4.2e-105	0.7096018735362998

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
269888	GH31_MGAM_SI_GAA	0.0	401	754	1	336	maltase-glucoamylase, sucrase-isomaltase, lysosomal acid alpha-glucosidase. This subgroup includes the following three closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), and lysosomal acid alpha-glucosidase (GAA), also known as acid-maltase. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end, and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII).
395838	Glyco_hydro_31	2.14e-143	383	751	2	319	Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.
269890	GH31_glucosidase_II_MalA	1.14e-106	401	754	1	305	Alpha-glucosidase II-like. Alpha-glucosidase II (alpha-D-glucoside glucohydrolase) is a glycosyl hydrolase family 31 (GH31) enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This subgroup also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source.
224418	YicI	9.04e-93	250	744	111	541	Alpha-glucosidase, glycosyl hydrolase family GH31 [Carbohydrate transport and metabolism].
269886	GH31_MGAM-like	1.67e-88	401	753	1	236	maltase-glucoamylase (MGAM)-like. This family includes the following closely related glycosyl hydrolase family 31 (GH31) enzymes: maltase-glucoamylase (MGAM), sucrase-isomaltase (SI), lysosomal acid alpha-glucosidase (GAA), neutral alpha-glucosidase C (GANC), the alpha subunit of neutral alpha-glucosidase AB (GANAB), and alpha-glucosidase II. MGAM is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion. SI is implicated in the digestion of dietary starch and major disaccharides such as sucrose and isomaltose, while GAA degrades glycogen in the lysosome, cleaving both alpha-1,4 and alpha-1,6 glucosidic linkages. MGAM and SI are anchored to small-intestinal brush-border epithelial cells. The absence of SI from the brush border membrane or its malfunction is associated with malabsorption disorders such as congenital sucrase-isomaltase deficiency (CSID). The domain architectures of MGAM and SI include two tandem GH31 catalytic domains, an N-terminal domain found near the membrane-bound end and a C-terminal luminal domain. Both of the tandem GH31 domains of MGAM and SI are included in this family. The domain architecture of GAA includes an N-terminal TFF (trefoil factor family) domain in addition to the GH31 catalytic domain. Deficient GAA expression causes Pompe disease, an autosomal recessive genetic disorder also known as glycogen storage disease type II (GSDII). GANC and GANAB are key enzymes in glycogen metabolism that hydrolyze terminal, non-reducing 1,4-linked alpha-D-glucose residues from glycogen in the endoplasmic reticulum. Alpha-glucosidase II is a GH31 enzyme, found in bacteria and plants, which has exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. Alpha-glucosidase II has been characterized in Bacillus thermoamyloliquefaciens where it forms a homohexamer. This family also includes the MalA alpha-glucosidase from Sulfolobus solfataricus and the AglA alpha-glucosidase from Picrophilus torridus. MalA is part of the carbohydrate-metabolizing machinery that allows this organism to utilize carbohydrates, such as maltose, as the sole carbon and energy source. The MGAM-like family corresponds to subgroup 1 in the Ernst et al classification of GH31 enzymes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBN19384.1|GH31	1.29e-203	192	754	61	628
ABR16166.1|GH31	1.82e-183	192	754	55	627
CAB4108661.1|GH31	7.50e-181	145	753	29	650
BBN19385.1|GH31	6.63e-180	192	754	59	632
CAG1864338.1|GH31	5.08e-179	162	754	33	634

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3W37_A	1.40e-171	192	754	73	638	Sugar beet alpha-glucosidase with acarbose [Beta vulgaris],3W38_A Sugar beet alpha-glucosidase [Beta vulgaris],3WEL_A Sugar beet alpha-glucosidase with acarviosyl-maltotriose [Beta vulgaris],3WEM_A Sugar beet alpha-glucosidase with acarviosyl-maltotetraose [Beta vulgaris],3WEN_A Sugar beet alpha-glucosidase with acarviosyl-maltopentaose [Beta vulgaris],3WEO_A Sugar beet alpha-glucosidase with acarviosyl-maltohexaose [Beta vulgaris]
3LPO_A	1.02e-130	159	744	75	631	Crystal structure of the N-terminal domain of sucrase-isomaltase [Homo sapiens],3LPO_B Crystal structure of the N-terminal domain of sucrase-isomaltase [Homo sapiens],3LPO_C Crystal structure of the N-terminal domain of sucrase-isomaltase [Homo sapiens],3LPO_D Crystal structure of the N-terminal domain of sucrase-isomaltase [Homo sapiens],3LPP_A Crystal complex of N-terminal sucrase-isomaltase with kotalanol [Homo sapiens],3LPP_B Crystal complex of N-terminal sucrase-isomaltase with kotalanol [Homo sapiens],3LPP_C Crystal complex of N-terminal sucrase-isomaltase with kotalanol [Homo sapiens],3LPP_D Crystal complex of N-terminal sucrase-isomaltase with kotalanol [Homo sapiens]
2QLY_A	1.08e-129	192	743	78	601	Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase [Homo sapiens],2QMJ_A Crystral Structure of the N-terminal Subunit of Human Maltase-Glucoamylase in Complex with Acarbose [Homo sapiens],3CTT_A Crystal complex of N-terminal Human Maltase-Glucoamylase with Casuarine [Homo sapiens]
3L4T_A	1.22e-129	192	743	78	601	Crystal complex of N-terminal Human Maltase-Glucoamylase with BJ2661 [Homo sapiens],3L4U_A Crystal complex of N-terminal Human Maltase-Glucoamylase with de-O-sulfonated kotalanol [Homo sapiens],3L4V_A Crystal complex of N-terminal Human Maltase-Glucoamylase with kotalanol [Homo sapiens],3L4W_A Crystal complex of N-terminal Human Maltase-Glucoamylase with miglitol [Homo sapiens],3L4X_A Crystal complex of N-terminal Human Maltase-Glucoamylase with NR4-8 [Homo sapiens],3L4Y_A Crystal complex of N-terminal Human Maltase-Glucoamylase with NR4-8II [Homo sapiens],3L4Z_A Crystal complex of N-terminal Human Maltase-Glucoamylase with Salacinol [Homo sapiens]
5NN3_A	8.01e-125	188	753	76	605	Crystal structure of human lysosomal acid-alpha-glucosidase, GAA [Homo sapiens],5NN5_A Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with 1-deoxynojirimycin [Homo sapiens],5NN6_A Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-hydroxyethyl-1-deoxynojirimycin [Homo sapiens],5NN8_A Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with acarbose [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9S7Y7|XYL1_ARATH	4.43e-173	192	753	61	632	Alpha-xylosidase 1 OS=Arabidopsis thaliana OX=3702 GN=XYL1 PE=1 SV=1
sp|O04931|AGLU_BETVU	1.24e-168	192	754	73	638	Alpha-glucosidase OS=Beta vulgaris OX=161934 PE=1 SV=1
sp|Q653V7|AGLU_ORYSJ	8.80e-168	164	754	34	610	Probable alpha-glucosidase Os06g0675700 OS=Oryza sativa subsp. japonica OX=39947 GN=Os06g0675700 PE=1 SV=1
sp|O04893|AGLU_SPIOL	6.34e-166	192	753	68	633	Alpha-glucosidase OS=Spinacia oleracea OX=3562 PE=1 SV=1
sp|Q43763|AGLU_HORVU	9.00e-162	195	754	59	604	Alpha-glucosidase OS=Hordeum vulgare OX=4513 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000063	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PHYSODRAFT_545197-t26_1-p1.