dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: CTMYA2_010960.t1-p1

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Basic Information help

Species

Candida tropicalis

Lineage

Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida tropicalis

CAZyme ID

CTMYA2_010960.t1-p1

CAZy Family

GH125

CAZyme Description

unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
672	CP047869\|CGC19	77403.48	5.4543

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CtropicalisMYA3404-2020	6136	N/A	0	6136

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	2.4.1.18:166	2.4.1.18:50

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	222	519	4e-145	0.9965870307167235

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200460	AmyAc_bac_euk_BE	0.0	153	563	2	406	Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic 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.
215246	PLN02447	0.0	7	672	60	733	1,4-alpha-glucan-branching enzyme
215519	PLN02960	5.84e-165	105	671	331	893	alpha-amylase
178782	PLN03244	3.54e-139	105	671	336	868	alpha-amylase; Provisional
223373	GlgB	7.31e-131	50	669	22	628	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits help

E-Value	Query Start	Query End	Hit Start
1	668	1	681
1	668	1	674
2	668	3	679
3	668	4	679
2	669	5	695

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.24e-285	9	668	31	696	Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_B Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_C Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens]
2.98e-282	16	668	6	664	Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLW_A Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens]
2.03e-236	9	665	13	688	Structure of the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
5.57e-236	9	665	12	687	Chain A, Isoform 2 of 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic [Oryza sativa Japonica Group]
5.76e-236	9	665	13	688	Structure of the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L [Oryza sativa Japonica Group],3VU2_B Structure of the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L [Oryza sativa Japonica Group]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
0.0	2	669	14	706	1,4-alpha-glucan-branching enzyme OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=GLC3 PE=3 SV=1
6.35e-300	6	667	10	702	1,4-alpha-glucan-branching enzyme OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=GLC3 PE=3 SV=1
4.47e-291	9	668	28	693	1,4-alpha-glucan-branching enzyme OS=Felis catus OX=9685 GN=GBE1 PE=2 SV=1
1.45e-290	8	667	15	680	1,4-alpha-glucan-branching enzyme OS=Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194) OX=747089 GN=GLC3 PE=2 SV=2
1.73e-289	8	669	11	680	1,4-alpha-glucan-branching enzyme OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=be1 PE=2 SV=3

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000057	0.000000

TMHMM Annotations help

There is no transmembrane helices in CTMYA2_010960.t1-p1.