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CAZyme Information: MGYG000003608_00589

You are here: Home > Sequence: MGYG000003608_00589

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 UBA4372 sp900770805
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; UBA4372; UBA4372 sp900770805
CAZyme ID MGYG000003608_00589
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
610 MGYG000003608_98|CGC1 68906.62 4.9456
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003608 1389684 MAG Fiji Oceania
Gene Location Start: 3841;  End: 5673  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003608_00589.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 61 351 5.6e-46 0.9653979238754326

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11314 AmyAc_arch_bac_plant_AmyA 5.53e-113 34 376 1 300
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. 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.
PLN02361 PLN02361 9.67e-47 34 428 13 396
alpha-amylase
PRK09441 PRK09441 1.40e-42 33 349 4 364
cytoplasmic alpha-amylase; Reviewed
PLN00196 PLN00196 1.17e-34 34 405 26 401
alpha-amylase; Provisional
PLN02784 PLN02784 6.70e-33 9 429 480 889
alpha-amylase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCS84551.1 4.88e-195 22 609 17 656
QNT66936.1 1.55e-186 24 609 19 670
QUB80123.1 5.00e-172 24 609 19 673
QUB41512.1 7.99e-172 24 609 2 655
QUB56692.1 8.24e-172 24 609 2 656

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1AMY_A 2.12e-37 34 412 2 385
CrystalAnd Molecular Structure Of Barley Alpha-Amylase [Hordeum vulgare],1AVA_A Amy2BASI PROTEIN-Protein Complex From Barley Seed [Hordeum vulgare],1AVA_B Amy2BASI PROTEIN-Protein Complex From Barley Seed [Hordeum vulgare],1BG9_A Barley Alpha-Amylase With Substrate Analogue Acarbose [Hordeum vulgare]
1HT6_A 1.55e-34 34 419 3 395
CrystalStructure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 [Hordeum vulgare],1P6W_A Crystal structure of barley alpha-amylase isozyme 1 (AMY1) in complex with the substrate analogue, methyl 4I,4II,4III-tri-thiomaltotetraoside (thio-DP4) [Hordeum vulgare],1RPK_A Crystal structure of barley alpha-amylase isozyme 1 (amy1) in complex with acarbose [Hordeum vulgare]
2QPS_A 1.55e-34 34 419 3 395
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare]
3WN6_A 2.08e-34 34 395 3 370
Crystalstructure of alpha-amylase AmyI-1 from Oryza sativa [Oryza sativa Japonica Group],3WN6_B Crystal structure of alpha-amylase AmyI-1 from Oryza sativa [Oryza sativa Japonica Group],3WN6_C Crystal structure of alpha-amylase AmyI-1 from Oryza sativa [Oryza sativa Japonica Group],3WN6_D Crystal structure of alpha-amylase AmyI-1 from Oryza sativa [Oryza sativa Japonica Group]
2QPU_A 2.89e-34 34 419 3 395
ChainA, Alpha-amylase type A isozyme [Hordeum vulgare],2QPU_B Chain B, Alpha-amylase type A isozyme [Hordeum vulgare],2QPU_C Chain C, Alpha-amylase type A isozyme [Hordeum vulgare]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8LFG1 2.90e-37 34 428 27 408
Probable alpha-amylase 2 OS=Arabidopsis thaliana OX=3702 GN=AMY2 PE=2 SV=1
P04063 1.79e-36 34 412 26 409
Alpha-amylase type B isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.2 PE=1 SV=3
P17654 1.38e-33 1 395 8 400
Alpha-amylase OS=Oryza sativa subsp. japonica OX=39947 GN=AMY1.1 PE=1 SV=2
P00693 5.05e-33 34 419 27 419
Alpha-amylase type A isozyme OS=Hordeum vulgare OX=4513 GN=AMY1.1 PE=1 SV=1
P17859 5.25e-33 34 414 25 407
Alpha-amylase OS=Vigna mungo OX=3915 GN=AMY1.1 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000277 0.999012 0.000177 0.000182 0.000173 0.000153

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003608_00589.