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CAZyme Information: MGYG000002633_01957

You are here: Home > Sequence: MGYG000002633_01957

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species TF01-11 sp003149875
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; TF01-11; TF01-11 sp003149875
CAZyme ID MGYG000002633_01957
CAZy Family GH13
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
754 MGYG000002633_40|CGC1 86863.21 5.4423
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002633 2903436 MAG China Asia
Gene Location Start: 11862;  End: 14126  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002633_01957.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 303 601 1.7e-114 0.9900332225913622

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11322 AmyAc_Glg_BE 0.0 241 638 6 402
Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1,4-alpha-glucan branching enzyme). The glycogen branching enzyme catalyzes the third step of glycogen biosynthesis by the cleavage of an alpha-(1,4)-glucosidic linkage and the formation a new alpha-(1,6)-branch by subsequent transfer of cleaved oligosaccharide. They are part of a group called branching enzymes which catalyze the formation of alpha-1,6 branch points in either glycogen or starch. This group includes proteins from bacteria, eukaryotes, and archaea. 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.
PRK12568 PRK12568 0.0 28 742 29 720
glycogen branching enzyme; Provisional
COG0296 GlgB 0.0 103 750 1 628
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
PRK05402 PRK05402 0.0 12 753 4 726
1,4-alpha-glucan branching protein GlgB.
PRK14705 PRK14705 0.0 9 748 503 1220
glycogen branching enzyme; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCN32019.1 6.21e-271 1 754 1 736
QHQ61835.1 5.45e-268 1 748 1 731
BCJ99479.1 3.22e-255 1 751 1 733
QRV19504.1 1.68e-252 1 754 1 746
ADL06402.1 1.68e-252 1 754 1 746

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GQW_A 3.31e-193 13 749 29 772
Crystalstructure of branching enzyme W610N mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142],5GQX_A Crystal structure of branching enzyme W610N mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142]
6KLF_A 4.00e-193 13 749 5 748
ChainA, 1,4-alpha-glucan branching enzyme GlgB [Crocosphaera subtropica ATCC 51142]
5GR5_A 9.35e-193 13 749 29 772
Crystalstructure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQZ_A 1.32e-192 13 749 29 772
Crystalstructure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQU_A 1.87e-192 13 749 29 772
Crystalstructure of branching enzyme from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142],5GQV_A Crystal structure of branching enzyme from Cyanothece sp. ATCC 51142 in complex with maltohexaose [Crocosphaera subtropica ATCC 51142],5GQY_A Crystal structure of branching enzyme from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8DLB8 1.02e-204 13 754 7 754
1,4-alpha-glucan branching enzyme GlgB OS=Thermosynechococcus vestitus (strain IAM M-273 / NIES-2133 / BP-1) OX=197221 GN=glgB PE=3 SV=1
Q3JCN0 1.71e-201 14 749 19 731
1,4-alpha-glucan branching enzyme GlgB OS=Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107) OX=323261 GN=glgB PE=3 SV=1
Q21M30 2.60e-198 14 749 9 726
1,4-alpha-glucan branching enzyme GlgB OS=Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) OX=203122 GN=glgB PE=3 SV=1
Q8YYX9 4.00e-198 13 754 10 757
1,4-alpha-glucan branching enzyme GlgB OS=Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) OX=103690 GN=glgB PE=3 SV=1
Q2JT08 1.37e-197 8 749 4 752
1,4-alpha-glucan branching enzyme GlgB OS=Synechococcus sp. (strain JA-3-3Ab) OX=321327 GN=glgB PE=3 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
1.000046 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002633_01957.