CAZyme Information: XP_001904330.1

Basic Information

• Species: Podospora anserina
• Lineage: Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora anserina
• CAZyme ID: XP_001904330.1
• CAZy Family: AA7
• CAZyme Description: Aamy domain-containing protein [Source:UniProtKB/TrEMBL;Acc:B2AF91]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
467		53047.25	6.4500

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PanserinaSmat	10888	515849	370	10518

• Gene Location: location=CU633457:1028243-1029871(+)

Full Sequence      

LLPSLSQLGITKIWIPPACKAADAKNGNGYDIYDLWDLGEFEQKGSTPTKWGSKAQLEEL
CRVAEGRGVKVLFDAVLNHKTGADYKERVKAKKVDPLDRNRELDGGEVREIESWTGFTFP
GRGGRYSGREWDRRHFTGVDWDDLTREKGVWKLGGKEWCVDVDEEVGNYDFLMFADVDHR
HPDVQQDAFDWVKWLPTQLKIGGLRLDAIKHYSFQFQKRLLRHIDDNVEKGKDWFIVGEY
WREDSEFLAKYIEYMDHRISLFDVPLCSNLSKISMAGERGDLRDLFKDALCLWKPNNVVT
PVAPWFLPHAYTLILLRANTGVPCVFWSDLYGSFASGPSSFIPPMSGNPTLLARLILIRK
LYAYGTQHDLFSHQHCVGFTREGHSAHGGGAGLAAVMGNQWGLSKLRMYVGKHHSGEKWI
DFLRLCPGEVMIDDEGWGEFPVSGNRGCSVWVSETAEGKDEVINLKL

Enzyme Prediction     

EC	3.2.1.1:2	3.2.1.116:1	2.4.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	5	332	2.9e-114	0.9912280701754386

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200457	AmyAc_bac_fung_AmyA	0.0	2	361	26	391	Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes bacterial and fungal proteins. 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.
236518	PRK09441	6.85e-168	3	452	29	479	cytoplasmic alpha-amylase; Reviewed
200453	AmyAc_arch_bac_plant_AmyA	9.16e-30	3	363	25	295	Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. 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.
395077	Alpha-amylase	1.62e-17	2	294	10	271	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
223443	AmyA	5.08e-17	2	337	35	326	Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDP29184.1|GH13_5	0.0	1	467	94	560
CAP62108.1|GH13_5	0.0	1	467	1	467
VBB80949.1|GH13_5	0.0	1	466	94	574
AEO58507.1|GH13_5	1.48e-213	2	460	1	463
QBZ66474.1|GH13_5	2.42e-163	2	465	69	540

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4UZU_A	2.30e-113	4	452	32	479	Three-dimensional structure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution [Geobacillus stearothermophilus]
1UD3_A	1.70e-110	4	454	31	480	Chain A, amylase [Bacillus sp. KSM-K38]
1UD2_A	1.70e-110	4	454	31	480	Crystal structure of calcium-free alpha-amylase from Bacillus sp. strain KSM-K38 (AmyK38) [Bacillus sp. KSM-K38],1UD4_A Crystal structure of calcium free alpha amylase from Bacillus sp. strain KSM-K38 (AmyK38, in calcium containing solution) [Bacillus sp. KSM-K38],1UD5_A Crystal structure of AmyK38 with rubidium ion [Bacillus sp. KSM-K38],1UD6_A Crystal structure of AmyK38 with potassium ion [Bacillus sp. KSM-K38],1UD8_A Crystal structure of AmyK38 with lithium ion [Bacillus sp. KSM-K38]
1HVX_A	9.68e-110	4	452	32	481	BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE [Geobacillus stearothermophilus]
1VJS_A	2.96e-109	5	444	32	474	Structure Of Alpha-Amylase Precursor [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P06279|AMY_GEOSE	2.67e-108	4	452	66	515	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
sp|P06278|AMY_BACLI	5.10e-108	5	444	61	503	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
sp|P19571|AMT6_BACS7	2.14e-105	4	454	66	518	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
sp|P00692|AMY_BACAM	5.35e-105	5	454	61	514	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
sp|P26612|AMY2_ECOLI	7.06e-94	6	454	32	492	Cytoplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=amyA PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000058	0.000000

TMHMM  Annotations     

There is no transmembrane helices in XP_001904330.1.