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CAZyme Information: MGYG000000432_00651

You are here: Home > Sequence: MGYG000000432_00651

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
Lineage Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-269;
CAZyme ID MGYG000000432_00651
CAZy Family GH57
CAZyme Description 1,4-alpha-glucan branching enzyme
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
528 61933.74 6.6003
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000432 1590144 MAG Sweden Europe
Gene Location Start: 58008;  End: 59594  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18 3.2.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH57 10 436 1.9e-78 0.8224543080939948

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10792 GH57N_AmyC_like 0.0 6 418 1 412
N-terminal catalytic domain of alpha-amylase ( AmyC ) and similar proteins. Alpha-amylases (alpha-1,4-glucan-4-glucanohydrolases, EC 3.2.1.1) play essential roles in alpha-glucan metabolism by catalyzing the hydrolysis of polysaccharides such as amylose starch, and beta-limit dextrin. This subfamily is represented by a novel alpha-amylase (AmyC) encoded by hyperthermophilic organism Thermotoga maritime ORF tm1438, and its prokaryotic homologs. AmyC functions as a homotetramer and shows thermostable amylolytic activity. It is strongly inhibited by acarbose. AmyC is composed of a N-terminal catalytic domain, containing a distorted TIM-barrel structure with a characteristic (beta/alpha)7 fold motif, and two additional less conserved domains. There are other two canonical alpha-amylases encoded from T. maritime that lack the sequence similarity to AmyC, and belong to a different superfamily.
COG1543 COG1543 0.0 4 527 1 501
Predicted glycosyl hydrolase, contains GH57 and DUF1957 domains [Carbohydrate transport and metabolism].
cd10816 GH57N_BE_TK1436_like 4.89e-113 6 418 1 423
N-terminal catalytic domain of Gh57 branching enzyme TK 1436 and similar proteins. The subfamily is represented by a novel branching-enzyme TK1436 of hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. Branching enzymes (BEs, EC 2.4.1.18) play a key role in synthesis of alpha-glucans and they generally are classified into glycoside hydrolase family 13 (GH13). However, TK1436 belongs to the GH57 family. It functions as a monomer and possesses BE activity. TK1436 is composed of a distorted N-terminal (beta/alpha)7-barrel domain and a C-terminal five alpha-helical domain, both of which participate in the formation of the active-site cleft.
cd01022 GH57N_like 1.41e-67 9 418 1 313
N-terminal catalytic domain of heat stable retaining glycoside hydrolase family 57. Glycoside hydrolase family 57(GH57) is a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57s cleave alpha-glycosidic bonds by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation.
pfam09210 DUF1957 2.07e-54 431 527 2 98
Domain of unknown function (DUF1957). This domain is found in a set of hypothetical bacterial proteins. Its exact function has not, as yet, been defined.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADG81752.1 4.14e-221 5 527 3 525
QSQ10341.1 2.82e-220 5 528 3 527
CAJ71922.1 8.38e-218 4 528 2 528
QII13593.1 8.38e-218 4 528 2 528
AEG15246.1 6.16e-217 5 528 3 525

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2B5D_X 1.56e-174 5 526 2 522
Crystalstructure of the novel alpha-amylase AmyC from Thermotoga maritima [Thermotoga maritima MSB8]
3N8T_A 5.51e-96 5 519 2 523
ChainA, alpha-amylase, GH57 family [Thermococcus kodakarensis],3N92_A Chain A, alpha-amylase, GH57 family [Thermococcus kodakarensis],3N98_A Chain A, alpha-amylase, GH57 family [Thermococcus kodakarensis]
5WU7_A 2.76e-94 5 519 2 525
Crystalstructure of GH57-type branching enzyme from hyperthermophilic archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3],5WU7_B Crystal structure of GH57-type branching enzyme from hyperthermophilic archaeon Pyrococcus horikoshii [Pyrococcus horikoshii OT3]
3P0B_A 7.58e-68 9 527 25 535
Thermusthermophilus family GH57 branching enzyme: crystal structure, mechanism of action and products formed [Thermus thermophilus]
1UFA_A 5.01e-67 9 527 5 515
Crystalstructure of TT1467 from Thermus thermophilus HB8 [Thermus thermophilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q5JDJ7 5.27e-94 5 519 2 523
1,4-alpha-glucan branching enzyme TK1436 OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1436 PE=1 SV=1
Q5SH28 2.63e-67 9 527 5 515
1,4-alpha-glucan branching enzyme TTHA1902 OS=Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) OX=300852 GN=TTHA1902 PE=1 SV=1
P9WQ26 1.57e-39 6 488 10 483
Probable 1,4-alpha-glucan branching enzyme MT3115 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT3115 PE=3 SV=1
P9WQ27 1.57e-39 6 488 10 483
Probable 1,4-alpha-glucan branching enzyme Rv3031 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv3031 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
1.000070 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000432_00651.