logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002278_00423

You are here: Home > Sequence: MGYG000002278_00423

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 Eubacterium_I ramulus_A
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eubacterium_I; Eubacterium_I ramulus_A
CAZyme ID MGYG000002278_00423
CAZy Family CBM48
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
597 MGYG000002278_2|CGC1 70305.99 5.9571
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002278 3656069 Isolate China Asia
Gene Location Start: 1036;  End: 2829  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 165 454 4.2e-125 0.9966777408637874
CBM48 18 93 8.6e-17 0.8421052631578947

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0296 GlgB 0.0 1 595 9 628
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
PRK05402 PRK05402 0.0 1 534 103 655
1,4-alpha-glucan branching protein GlgB.
PRK12313 PRK12313 0.0 1 562 10 587
1,4-alpha-glucan branching protein GlgB.
cd11322 AmyAc_Glg_BE 0.0 99 490 1 402
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.
TIGR01515 branching_enzym 0.0 2 526 1 541
alpha-1,4-glucan:alpha-1,4-glucan 6-glycosyltransferase. This model describes the glycogen branching enzymes which are responsible for the transfer of chains of approx. 7 alpha(1--4)-linked glucosyl residues to other similar chains (in new alpha(1--6) linkages) in the biosynthesis of glycogen. This enzyme is a member of the broader amylase family of starch hydrolases which fold as (beta/alpha)8 barrels, the so-called TIM-barrel structure. All of the sequences comprising the seed of this model have been experimentally characterized. This model encompasses both bacterial and eukaryotic species. No archaea have this enzyme, although Aquifex aolicus does. Two species, Bacillus thuringiensis and Clostridium perfringens have two sequences each which are annotated as amylases. These annotations are aparrently in error. GP|18143720 from C. perfringens, for instance, contains the note "674 aa, similar to gp:A14658_1 amylase (1,4-alpha-glucan branching enzyme (EC 2.4.1.18) ) from Bacillus thuringiensis (648 aa); 51.1% identity in 632 aa overlap." A branching enzyme from Porphyromonas gingivales, OMNI|PG1793, appears to be more closely related to the eukaryotic species (across a deep phylogenetic split) and may represent an instance of lateral transfer from this species' host. A sequence from Arabidopsis thaliana, GP|9294564, scores just above trusted, but appears either to contain corrupt sequence or, more likely, to be a pseudogene as some of the conserved catalytic residues common to the alpha amylase family are not conserved here. [Energy metabolism, Biosynthesis and degradation of polysaccharides]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QBF75938.1 3.23e-316 1 592 1 591
QRO35728.1 3.23e-316 1 592 1 591
QYX25725.1 3.79e-315 1 592 1 591
CBL24631.1 1.47e-307 1 593 1 591
QEK16660.1 1.24e-299 1 596 1 595

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GQW_A 1.69e-156 2 542 133 713
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]
5GR5_A 2.38e-156 2 542 133 713
Crystalstructure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQU_A 4.74e-156 2 542 133 713
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]
5GR2_A 1.33e-155 2 542 133 713
Crystalstructure of branching enzyme L541A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142],5GR4_A Crystal structure of branching enzyme L541A mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142]
5GQZ_A 1.88e-155 2 542 133 713
Crystalstructure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142 [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
P30537 1.53e-182 1 562 9 578
1,4-alpha-glucan branching enzyme GlgB OS=Bacillus caldolyticus OX=1394 GN=glgB PE=1 SV=1
P30538 2.06e-181 1 559 9 575
1,4-alpha-glucan branching enzyme GlgB OS=Geobacillus stearothermophilus OX=1422 GN=glgB PE=1 SV=1
Q8RF62 5.56e-177 1 542 8 548
1,4-alpha-glucan branching enzyme GlgB OS=Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355) OX=190304 GN=glgB PE=3 SV=1
A7GUA1 1.19e-176 6 559 14 575
1,4-alpha-glucan branching enzyme GlgB OS=Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98) OX=315749 GN=glgB PE=3 SV=1
Q65FS4 5.32e-176 6 597 14 620
1,4-alpha-glucan branching enzyme GlgB OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 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
1.000065 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002278_00423.