logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003491_00325

You are here: Home > Sequence: MGYG000003491_00325

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 UBA2804 sp900768635
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Succinivibrionaceae; UBA2804; UBA2804 sp900768635
CAZyme ID MGYG000003491_00325
CAZy Family GH13
CAZyme Description Periplasmic alpha-amylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
724 MGYG000003491_34|CGC3 81469.82 7.7879
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003491 2438052 MAG Fiji Oceania
Gene Location Start: 50830;  End: 53004  Strand: -

Full Sequence      Download help

MSKFKLSAAA  SLLAVLATVG  QVSQAATEYE  FKNPVYVYVD  GKMVSSAEFK  KSGSMNYLFE60
ATVSLDKGEH  SIMLADQNKT  CDGSFAPDVS  EAGRLTFGKN  FKMATCAKNK  SVPLKILLPG120
NYTFTISMFN  PKTPTVKVLR  ATGGEVTIKR  EVPKVKCLTY  KGGVVNVDVA  GTWPEGTMLR180
DAYSGALAKV  TKGKVRIVPD  ARSEGLVLLE  PATEESRTQK  PFSWDNAIVY  FLLTDRFNNG240
DKSNDNSFGR  QKDGKDEIGT  FHGGDFKGII  QKLDYLKQLG  VNALWITPMV  EQSHGYVGGG300
DENHSFPFYG  YHGYWAADFT  RLDPNFGTDE  DLRNLVKECH  KRGIRLVVDT  VMNHAGYATL360
ADLQDFGLES  VTKNTSSLPD  RWADYKPKNM  ANWQGYSQFI  NYNSAGWLDW  WGNKWIRAGF420
PHHQSPGTDD  QNMAVGGLPD  FITESKEFVS  LPKFLKNKKD  TRAKDLPNAT  VLDYLVSWHT480
YWVRNFGIDG  LRCDTAKHIQ  AEGWKKLRDS  AGSALEAWKK  ENPSEKLDDS  SLFMVGEVWD540
HGLTRNALYY  DNGFDSLINF  DYQKMSLQFA  QCFADADYTY  TNYAKRINSD  PTFNALSYIS600
SHDTKLFWGD  FKDFGLQKRA  ANGLLMLPGQ  VQIYYGDESG  RGLMPDGGYP  DQALRSDMNW660
DDLRKPEYRD  LFQHWSKLNH  FRLNHPAVAE  GSHRQISNAK  SPYYAFVREK  GNDKVMVVFV720
GNRP724

Enzyme Prediction      help

No EC number prediction in MGYG000003491_00325.

CAZyme Signature Domains help

Created with Snap3672108144181217253289325362398434470506543579615651687264639GH13
Family Start End Evalue family coverage
GH13 264 639 2.4e-142 0.9972222222222222

CDD Domains      download full data without filtering help

Created with Snap367210814418121725328932536239843447050654357961565168758723malS228685AmyAc_bac_CMD_like_2226692AmyAc_CMD224682AmyAc_euk_AmyA264691AmyAc_bac2_AmyA
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK09505 malS 0.0 58 723 35 683
alpha-amylase; Reviewed
cd11339 AmyAc_bac_CMD_like_2 1.33e-63 228 685 4 344
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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.
cd11338 AmyAc_CMD 7.44e-57 226 692 1 388
Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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.
cd11319 AmyAc_euk_AmyA 1.25e-55 224 682 6 369
Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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.
cd11316 AmyAc_bac2_AmyA 2.02e-52 264 691 20 403
Alpha amylase catalytic domain found in 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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.

CAZyme Hits      help

Created with Snap36721081441812172532893253623984344705065435796156516872723QXW28522.1|GH13_1913723AUY08893.1|GH13_1913723QUM02581.1|GH13_1935724ATP08579.1|GH13_1913723BBT54116.1|GH13_19
Hit ID E-Value Query Start Query End Hit Start Hit End
QXW28522.1 3.49e-285 2 723 5 706
AUY08893.1 2.07e-284 13 723 16 706
QUM02581.1 4.17e-284 13 723 16 706
ATP08579.1 5.12e-284 35 724 30 703
BBT54116.1 5.91e-284 13 723 16 706

PDB Hits      download full data without filtering help

Created with Snap36721081441812172532893253623984344705065435796156516872236915A2A_A2166915A2B_A2237224E2O_A2207181EA9_C2197181SMA_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
5A2A_A 1.69e-38 223 691 5 370
CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A 1.83e-38 216 691 34 404
CrystalStructure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A 7.80e-38 223 722 6 400
Crystalstructure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
1EA9_C 1.04e-32 220 718 123 531
Cyclomaltodextrinase[Bacillus sp. (in: Bacteria)],1EA9_D Cyclomaltodextrinase [Bacillus sp. (in: Bacteria)]
1SMA_A 3.57e-31 219 718 127 534
CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]

Swiss-Prot Hits      download full data without filtering help

Created with Snap3672108144181217253289325362398434470506543579615651687115723sp|P25718|AMY1_ECOLI209722sp|P21543|AMYB_PAEPO199718sp|Q08341|CDAS_LYSSH220718sp|Q59226|CDAS_BACSP259708sp|Q05884|AMY_STRLI
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P25718 6.95e-182 115 723 83 676
Periplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=malS PE=1 SV=1
P21543 6.37e-39 209 722 729 1145
Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
Q08341 7.84e-33 199 718 106 533
Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1
Q59226 4.53e-32 220 718 123 531
Cyclomaltodextrinase OS=Bacillus sp. OX=1409 GN=CDI5 PE=1 SV=1
Q05884 5.12e-32 259 708 93 547
Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 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
0.000311 0.998860 0.000250 0.000195 0.000189 0.000179

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003491_00325.