CAZyme Information: AGR57_511T0-p1

Basic Information

• Species: Phanerochaete chrysosporium
• Lineage: Basidiomycota; Agaricomycetes; ; Phanerochaetaceae; Phanerochaete; Phanerochaete chrysosporium
• CAZyme ID: AGR57_511T0-p1
• CAZy Family: GH38
• CAZyme Description: Glycoside Hydrolase Family 13 / Glycosyltransferase Family 5 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2342		261970.76	5.7797

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PchrysosporiumRP-78	13602	273507	0	13602

• Gene Location: location=PchrRP-78_SC001:1066671-1074347(-)

Full Sequence      

MRLFKAALSLLTVASFVCASPYRDDLVDYNINTNQNAQSPTEYTTNKRASYTPSPPNWRE
IPFYTILLDKFADGDPSNNDYFGTVYEWDWRETQLRFGGDLKGLVSKLDYLQGMGIRGIF
ISGTPFINMLWQADSYSPLDFTVLDPHWGTLADWQQTIDEIHARGMYIMADFTVGTMGDL
VGFDGYLNTSAPFDLHEHNAVWKHPRYAPWGFDEYKDFVINNTWNTSCQLPPLWSNDGSQ
ENVGWGGGCMESDFDQYGDMEAFGVHPDWQRQLSKFASVQDRLREWRPSVMDKLKTFACM
TITALDIDAIRIDKSTQVTVDALAEWASSARACAHALGKTNFFITGEVTGGDTFGALYYG
RGRTPTQLPPGFLAAANLSANENQFFLRDAPLNGLDAVAFHYSIYRSLTRFLGMDGNLQV
AYDIDVNFVTAWNQMFVTNDFLNANGTLDPRHMYGTSNFDVFRWPSLENGTQRSVLGTFI
TSLVMPGIPLLYYGEEQNFYLYDTGASNYLYGRQAMISNKAWQRHGCYALGSQQYFNMPL
DKSLVGCHDDWNSLDHFDPTTDSRRVFARFNQLRSIYNALQDGFNLVQRGNWTYKIERPG
SNDTPTEMGLWSVSRSGIPGSQTLGGNHTDQVWLLYTNENRTRTWEYDCKDKDHWMSSPY
QAGQTVRNLVAPYETYTLAESLSSYYNDGKAPYTGCMASLTTQPFGFLALVPEEEWVGPN
PTLTGFRPGHDARIHAESTDANATVVDITLEFNMPMDCNSVTQSLSFNMSSSGHGSAPTI
NQGSINCTNIANPVFSTINGVDASMWSWSATLEGVPDGILEILVNNPSAPNGAGSTGSKD
RLLLRKGSAKNVMVFPESDYDNDAFGYSNGQYTFTHQAFGADKFRYSTNFGQNWTEWRNW
EDTTTIDEKEFEGNFWEGQHIMVQYWSALAASAAVVVHADRGYPKPRRVPQFLARGPFNQ
WGFDQGIPAEMTHNDDGKWELEIMATWPTYVQLNVWGYDDYYYGDVDSDGVLDRLPPNTA
APNYLNMSAPPHPHLAWALLVDDATLTWTLEPRGQSAVGAIMYALLLSIPLITGTLAVVI
FMWSFYGIKYNKWGVKPTKEHNYFPILGALGHKSSANLSKEHMSEKVFGGHHKQTEIIGW
PEDKNKRRKVLIATLEYEIIDWKLKVKIGGLGVMSSLMGKAMTDVDLVWVIPKVKDLEYP
PGEPAEPIEVIIFGEPYLIEVETHVLDNITYVILDSPVFRAQTKSDPYPARMDDLSSAIF
YSTWNQAIAATVKRFPLIDIYHINDYHGALAPIYLLPKVLPVCLSLHNAEFQGLWPLRTK
EEMKEVCSAFNISKEHCTKYVQFGNTFNLLHAAASFISVHQKSVGVAGVSDKYGKRSWAR
YPALWTLKHIDSLPNPDPTDIAALDENPVSVRDIKIDEAAEAERPEHKRQAQEWAGIKQD
PNADLFVFVGRWSKQKGVDIIADVMPSLLEKRPSIQLIAVGPVIDLYGRFAAEKLNRLME
MYPDRVYSKPEFTALPPYLFSGADFALIPSRDEPFGLVAVEFGRKGALGVGSRLGGLGLM
PGWWFPVESTSTEHMISQLTKTIKMALKSTEEERAMLRARSAVQRFPVVEWRQRMEDFHR
RSITMSRSLAGPNAFRASDCDGGRGHAIAEHDDWNPEYQAHPSQPAWDAASINESPRTPG
PPSSPGQWSQDTLTPGQDGLHAPPRLLPDGRRGSFSTDVSDNEGDYFTQNRASTDNRQDF
GNFLERANKTIARDNKHAPDPFLDAAPSRPFGSHSRVSSVESIASIVTEKADSPLNKAMA
AFTDADGGVTAEFAQKLQALNAHNSKHELSIEKFLTKSEEAFFDKVKKDKLSSAASIRSS
QRDSVWGTPAPSSFDHSRPSSPSQSGFTGADGYSGALPDHQDVVIMTGLQIAMAREIGGW
PIYTIIIAAGQMLSATSFQITLLSGQNWQTDLQLYVLGGVFLASSAVWYVLFRYKPSVYC
LSAPWLFFGLAFFLIGLPSVTPALHGAHDILTSIATWAYAVASSAAFIFFGLNFGEEAGA
ATEVWTMRACIVQGSQQIWVAALWYWGNHLNGSVSTAMAPWWIVLIVWPLALISGLFAYL
MLYGLPDYYRQTPPKVPNFLKTLFRRKLVLWFLGSEILRDYWLSGPYGRNWSFLWAVPIP
KWQILLLVIAFFIGVWAIMMYILTFFSKTHTWLLPVFAVGLGAPRWCQMLWGTSSLALYI
PWAGHAGPYLGISLWLWLGVLDAIQGVGLGMILLQTLSRLHVCATLAFAQIIGSICVMVA
RATAPNKVGPESVFPDAAKWDFQDGLKGSPMASAPFWIAMICQIVIVIGYFWFYRKEQLA
RP

Enzyme Prediction     

EC	2.4.1.183:18	2.4.1.-:2	2.4.1.183:36	2.4.1.-:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	98	498	2.7e-171	0.9975
GH13	1149	1615	4e-95	0.985

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200462	AmyAc_AGS	0.0	6	577	1	569	Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine diphosphoglucose-1,3-alpha-glucan glucosyltransferase and 1,3-alpha-D-glucan synthase). Alpha 1,3-glucan synthase (AGS, EC 2.4.1.183) is an enzyme that catalyzes the reversible chemical reaction of UDP-glucose and [alpha-D-glucosyl-(1-3)]n to form UDP and [alpha-D-glucosyl-(1-3)]n+1. AGS is a component of fungal cell walls. The cell wall of filamentous fungi is composed of 10-15% chitin and 10-35% alpha-1,3-glucan. AGS is triggered in fungi as a response to cell wall stress and elongates the glucan chains in cell wall synthesis. This group includes proteins from Ascomycetes and Basidomycetes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
340822	GT5_Glycogen_synthase_DULL1-like	4.01e-106	1149	1614	1	464	Glycogen synthase GlgA and similar proteins. This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
223443	AmyA	2.01e-35	63	604	3	476	Glycosidase [Carbohydrate transport and metabolism].
223374	GlgA	5.63e-33	1917	2320	119	487	Glycogen synthase [Carbohydrate transport and metabolism].
200489	AmyAc_5	1.58e-31	63	516	2	411	Alpha amylase catalytic domain found in an uncharacterized protein family. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDK64594.1|GH13_22|GT5	0.0	68	2342	1	2293
QRW14378.1|GH13_22|GT5	0.0	8	2342	10	2353
QRV99867.1|GH13_22|GT5	0.0	8	2342	10	2353
QRV85802.1|GH13_22|GT5	0.0	8	2342	10	2353
QRW27711.1|GH13_22|GT5	0.0	21	2342	2	2309

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	2.37e-20	58	496	6	327	Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	3.39e-20	58	496	40	361	Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A	1.78e-19	58	496	7	328	Crystal structure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
3D1J_A	6.03e-16	1279	1557	131	401	Chain A, Glycogen synthase [Escherichia coli]
2QZS_A	6.29e-16	1279	1557	131	401	Crystal Structure of Wild-type E.coli GS in complex with ADP and Glucose(wtGSb) [Escherichia coli],2R4T_A Crystal Structure of Wild-type E.coli GS in Complex with ADP and Glucose(wtGSc) [Escherichia coli],2R4U_A Crystal Structure of Wild-type E.coli GS in complex with ADP and Glucose(wtGSd) [Escherichia coli],3GUH_A Crystal Structure of Wild-type E.coli GS in complex with ADP and DGM [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9USK8|AGS1_SCHPO	0.0	7	2342	15	2410	Cell wall alpha-1,3-glucan synthase ags1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ags1 PE=1 SV=3
sp|Q09854|MOK11_SCHPO	0.0	18	2342	22	2397	Cell wall alpha-1,3-glucan synthase mok11 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok11 PE=3 SV=2
sp|Q9UUL4|MOK12_SCHPO	0.0	17	2340	20	2351	Cell wall alpha-1,3-glucan synthase mok12 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok12 PE=3 SV=1
sp|Q9Y719|MOK13_SCHPO	0.0	10	2342	12	2358	Cell wall alpha-1,3-glucan synthase mok13 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok13 PE=3 SV=2
sp|Q9Y704|MOK14_SCHPO	2.34e-300	1029	2342	147	1369	Cell wall alpha-1,3-glucan synthase mok14 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok14 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000361	0.999592	CS pos: 19-20. Pr: 0.9746

TMHMM  Annotations     

Start	End
1060	1082
1920	1942
1952	1971
1978	2000
2010	2032
2044	2066
2081	2103
2164	2186
2219	2241
2262	2284
2312	2334