dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002022_00105

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Basic Information help

Species

Centipeda artemidis

Lineage

Bacteria; Firmicutes_C; Negativicutes; Selenomonadales; Selenomonadaceae; Centipeda; Centipeda artemidis

CAZyme ID

MGYG000002022_00105

CAZy Family

GH13

CAZyme Description

Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1149	MGYG000002022_1\|CGC1	132734.01	5.2795

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002022	2160973	MAG	Spain	Europe

Gene Location

Start: 106297; End: 109746 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002022_00105.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH77	664	1140	4.7e-168	0.97165991902834
GH13	191	523	4.7e-134	0.9936708860759493

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam02446	Glyco_hydro_77	0.0	664	1125	1	455	4-alpha-glucanotransferase. These enzymes EC:2.4.1.25 transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1,4)-alpha-D-glucan.
PRK14510	PRK14510	0.0	9	1128	5	1193	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
cd11338	AmyAc_CMD	0.0	138	560	1	389	Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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.
PRK14508	PRK14508	0.0	658	1149	5	496	4-alpha-glucanotransferase; Provisional
PLN02635	PLN02635	1.71e-171	639	1149	12	525	disproportionating enzyme

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
QNH53465.1	1	1149	1	1149
ANR69627.1	1	1149	1	1149
AOH47405.1	1	1149	1	1149
AKT53142.1	1	1149	1	1149
AME04250.1	1	1149	1	1149

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2X1I_A	9.98e-136	661	1143	8	493	glycosidehydrolase family 77 4-alpha-glucanotransferase from thermus brockianus [Thermus brockianus]
2OWC_A	2.09e-135	658	1143	8	495	Structureof a covalent intermediate in Thermus thermophilus amylomaltase [Thermus thermophilus],2OWW_A Covalent intermediate in amylomaltase in complex with the acceptor analog 4-deoxyglucose [Thermus thermophilus],2OWX_A THERMUS THERMOPHILUS AMYLOMALTASE AT pH 5.6 [Thermus thermophilus]
1CWY_A	2.74e-135	658	1143	5	493	CrystalStructure Of Amylomaltase From Thermus Aquaticus, A Glycosyltransferase Catalysing The Production Of Large Cyclic Glucans [Thermus aquaticus],1ESW_A X-Ray Structure Of Acarbose Bound To Amylomaltase From Thermus Aquaticus. Implications For The Synthesis Of Large Cyclic Glucans [Thermus aquaticus]
1FP8_A	3.85e-135	658	1143	5	493	StructureOf The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 [Thermus thermophilus],1FP9_A Structure Of Amylomaltase From Thermus Thermophilus Hb8 In Space Group C2 [Thermus thermophilus]
5JIW_A	1.57e-133	658	1143	5	493	Crystalstructure of Thermus aquaticus amylomaltase (GH77) in complex with a 34-meric cycloamylose [Thermus aquaticus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P0A3Q1	4.75e-145	657	1149	3	495	4-alpha-glucanotransferase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=malQ PE=3 SV=1
P0A3Q0	4.75e-145	657	1149	3	495	4-alpha-glucanotransferase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malQ PE=3 SV=1
O87172	1.50e-134	658	1143	5	493	4-alpha-glucanotransferase OS=Thermus thermophilus OX=274 GN=malQ PE=1 SV=1
P72785	8.03e-131	657	1132	4	482	4-alpha-glucanotransferase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=malQ PE=3 SV=1
O66937	9.15e-129	658	1131	2	467	4-alpha-glucanotransferase OS=Aquifex aeolicus (strain VF5) OX=224324 GN=malQ PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000032	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000002022_00105.