dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Pneumocystis jirovecii

Lineage

Ascomycota; Pneumocystidomycetes; ; Pneumocystidaceae; Pneumocystis; Pneumocystis jirovecii

CAZyme ID

PNEJI1_000567-t26_1-p1

CAZy Family

GH31

CAZyme Description

unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1786	CAKM01000257\|CGC1	205766.31	6.5757

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PjiroveciiSE8	3752	1209962	217	3535

Gene Location

Enzyme Prediction help

EC	2.4.1.25:2	3.2.1.33:2	2.4.1.25:22	3.2.1.33:21	2.4.1.25:22	3.2.1.33:21

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	1350	1773	9.8e-177	0.9930875576036866

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200466	AmyAc_Glg_debranch_2	0.0	419	902	1	478	Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities, 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. The catalytic triad (DED), which is highly conserved in other debranching enzymes, is not present in this group. 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.
273673	glyc_debranch	0.0	349	1779	42	1464	glycogen debranching enzymye. glycogen debranching enzyme possesses two different catalytic activities; oligo-1,4-->1,4-glucantransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). Site directed mutagenesis studies in S. cerevisiae indicate that the transferase and glucosidase activities are independent and located in different regions of the polypeptide chain. Proteins in this model belong to the larger alpha-amylase family. The model covers eukaryotic proteins with a seed composed of human, nematode and yeast sequences. Yeast seed sequence is well characterized. The model is quite rigorous; either query sequence yields large bit score or it fails to hit the model altogether. There doesn't appear to be any middle ground. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
405401	hDGE_amylase	0.0	435	870	3	439	Glycogen debranching enzyme, glucanotransferase domain. This is a glucanotransferase catalytic domain of the eukaryotic variant of the glycogen debranching enzyme (GDE). The eukaryotic GDEs performs two functions: 4-alpha-D-glucanotransferase, EC:2.4.1.25, and Amylo-alpha-1,6-glucosidase, EC:3.2.1.33, performed by the, respectively N- and C- terminal halves of eukaryotic GDE enzymes. The domain is a catalytic domain responsible for the glucanotransferase function. It belongs to the alpha-amylase clan and is predicted to have a structure of a 8-stranded alpha/beta barrel (TIM barrel) where strands are interrupted by long loops and additional mini-domains. In most other amylases, the catalytic domain is followed by a beta- barrel substrate binding domain, but presence of such a domain cannot be verified in the human (and other eukaryotic) GDE enzymes.
396646	Cytochrom_C1	4.59e-128	66	284	1	219	Cytochrome C1 family.
405402	hGDE_central	1.52e-114	1022	1258	1	242	Central domain of human glycogen debranching enzyme. This is a central domain of the eukaryotic variant of the glycogen debranching enzyme (GDE). The eukaryotic GDE performs two functions: 4-alpha-D-glucanotransferase, EC:2.4.1.25, and Amylo-alpha-1,6-glucosidase, EC:3.2.1.33, performed by the, respectively N- and C- terminal halves of eukaryotic GDE enzyme This central domain follows the glucanotransferase domain and precedes the glucosidase (GDE_N) domain. It is very likely that the current definition contains two or more domains, by analogy with baterial GDEs, this domain should be involved in substrate- binding either for the N-terminal glucanotransferase and/or the the C-terminal glucosidase (or both).

CAZyme Hits help

E-Value	Query Start	Query End	Hit Start
300	1782	1	1437
300	1780	1	1513
300	1786	1	1548
300	1786	1	1548
300	1786	1	1548

PDB Hits download full data without filtering help

E-Value	Query Start	Query End	Hit Start	Hit End
310	1779	28	1522	Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme (E564Q) in complex with maltopentaose [[Candida] glabrata CBS 138],5D0F_B Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme (E564Q) in complex with maltopentaose [[Candida] glabrata CBS 138]
310	1779	28	1522	Chain A, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138],7EKX_B Chain B, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138]
310	1779	28	1522	Chain A, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138],7EKW_B Chain B, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138]
310	1779	28	1522	Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme [[Candida] glabrata CBS 138],5D06_B Crystal Structure of the Candida Glabrata Glycogen Debranching Enzyme [[Candida] glabrata CBS 138]
310	1779	28	1522	Chain A, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138],7EKU_B Chain B, 4-alpha-glucanotransferase [[Candida] glabrata CBS 138]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
0.0	308	1779	7	1528	Glycogen debranching enzyme OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GDB1 PE=1 SV=1
8.75e-302	353	1777	49	1532	Glycogen debranching enzyme OS=Equus caballus OX=9796 GN=AGL PE=2 SV=1
5.93e-298	353	1777	49	1531	Glycogen debranching enzyme OS=Homo sapiens OX=9606 GN=AGL PE=1 SV=3
9.28e-297	353	1777	49	1532	Glycogen debranching enzyme OS=Canis lupus familiaris OX=9615 GN=AGL PE=2 SV=1
1.45e-294	353	1777	72	1554	Glycogen debranching enzyme OS=Oryctolagus cuniculus OX=9986 GN=AGL PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000018	0.000011

TMHMM Annotations download full data without filtering help

Start	End
20	42
259	276

You are here: Home > Sequence: PNEJI1_000567-t26_1-p1