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CAZyme Information: MGYG000000490_01606

You are here: Home > Sequence: MGYG000000490_01606

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 UMGS1865 sp900768535
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS1865; UMGS1865 sp900768535
CAZyme ID MGYG000000490_01606
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
645 72026.36 5.0019
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000490 2369759 MAG Fiji Oceania
Gene Location Start: 5137;  End: 7074  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000490_01606.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 262 547 1.3e-27 0.882943143812709

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11313 AmyAc_arch_bac_AmyA 7.87e-27 249 563 15 303
Alpha amylase catalytic domain found in archaeal and bacterial 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 firmicutes, bacteroidetes, and proteobacteria. 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.
cd00551 AmyAc_family 1.27e-17 236 544 2 253
Alpha amylase catalytic domain family. 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; and 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 this 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.
pfam00128 Alpha-amylase 2.01e-14 262 547 10 325
Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
COG0366 AmyA 7.53e-13 239 619 12 495
Glycosidase [Carbohydrate transport and metabolism].
cd14791 GH36 1.34e-11 305 429 66 184
glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QHT61281.1 1.20e-107 9 615 29 648
AEE96957.1 6.42e-107 27 643 47 680
AZN42601.1 1.04e-106 10 642 33 695
QKG58678.1 1.16e-17 235 643 44 475
AZI32560.1 1.65e-17 249 548 36 316

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5OT1_A 4.91e-09 235 390 339 503
ChainA, Pullulanase type II, GH13 family [Thermococcus kodakarensis]
4LPC_A 6.27e-07 247 390 141 289
CrystalStructure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LPC_B Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LPC_C Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LPC_D Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LQ1_A Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],4LQ1_B Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],4LQ1_C Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],4LQ1_D Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],5E6Y_A Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Y_B Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Y_C Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Y_D Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_A Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_B Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_C Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_D Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_A Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_B Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_C Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_D Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A]
1M7X_A 6.30e-07 247 390 146 294
TheX-ray Crystallographic Structure of Branching Enzyme [Escherichia coli],1M7X_B The X-ray Crystallographic Structure of Branching Enzyme [Escherichia coli],1M7X_C The X-ray Crystallographic Structure of Branching Enzyme [Escherichia coli],1M7X_D The X-ray Crystallographic Structure of Branching Enzyme [Escherichia coli]
1GJU_A 8.43e-07 254 343 118 221
Maltosyltransferasefrom Thermotoga maritima [Thermotoga maritima MSB8],1GJW_A Thermotoga maritima maltosyltransferase complex with maltose [Thermotoga maritima]
7D9B_A 1.41e-06 241 392 162 347
ChainA, Alpha-glycosidase [Weissella cibaria]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
L8B068 3.98e-10 262 611 274 616
Alpha-amylase MalA OS=Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1) OX=1227453 GN=malA PE=1 SV=1
Q3STC2 7.24e-10 236 610 239 652
1,4-alpha-glucan branching enzyme GlgB OS=Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255) OX=323098 GN=glgB PE=3 SV=1
Q8PQA2 5.00e-09 253 390 259 398
1,4-alpha-glucan branching enzyme GlgB 2 OS=Xanthomonas axonopodis pv. citri (strain 306) OX=190486 GN=glgB2 PE=3 SV=1
Q3BYI0 5.08e-09 253 390 283 422
1,4-alpha-glucan branching enzyme GlgB 2 OS=Xanthomonas campestris pv. vesicatoria (strain 85-10) OX=316273 GN=glgB2 PE=3 SV=1
Q4UZL7 2.63e-08 262 390 276 408
1,4-alpha-glucan branching enzyme GlgB 2 OS=Xanthomonas campestris pv. campestris (strain 8004) OX=314565 GN=glgB2 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
0.999988 0.000043 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000490_01606.