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CAZyme Information: MGYG000003319_00677

You are here: Home > Sequence: MGYG000003319_00677

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; Oscillospirales; Ruminococcaceae; Ruminiclostridium_E;
CAZyme ID MGYG000003319_00677
CAZy Family GH13
CAZyme Description Amylopullulanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
622 71267.31 4.9927
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003319 1809679 MAG United Republic of Tanzania Africa
Gene Location Start: 460;  End: 2328  Strand: -

Full Sequence      Download help

MLPIYDAFSE  SYKTPFGAVA  SGTEIEFKLR  FPVDVLVEEV  MLVSYRPGYK  ERFVHLDLSE60
TTDSFKMFSC  KYAPEDVGLH  YYYFSLLLNR  NRHYVKKSGA  SLGVIDNGEL  FQLTVYAKDM120
TTPDWLKGGV  MYQIFPDRFA  KSGIYHDNVP  ADRQLHTDWL  ETPVWKPDSR  GQITNNDYFG180
GDLKGIEQKL  PYLESLGVTV  IYLNPIFESH  ENHRYCTADY  SKIDPLLGTE  EDFVSLCKAA240
ADRGIKIILD  GVFSHTGADS  VYFNKFGRYG  ENTGAYRDPN  SPYREWYSFS  NYPNTYESWW300
GITTLPNVIE  NNPAYTNYIC  GDGGILQKWL  DLGASGWRLD  VADELPDEFI  DNLNKAVKAN360
GSDKVIYGEV  WEDATNKESY  GVRRRYLIGG  QLDSVMNYPF  KEAILNYVKT  GNPQELTEGI420
MTIVEHYPKP  CTDILMNFLS  THDTERAITR  LAGEEVGWNG  REWQAERYLT  DEQFVFGITL480
MRCAMVLQFF  LPGIPCIYYA  DEAGQEGYKD  PFNRRTYPWG  SEDERLIDFT  KRLGHLRRSI540
KAFAKGNLHF  IEVTKEYAVF  SRTDREIGEQ  AVVIMNRSRR  VVERQIDCLA  EYRNAAVVHG600
TSCSDGTIRV  SPFDFGLIVS  KE622

Enzyme Prediction      help

No EC number prediction in MGYG000003319_00677.

CAZyme Signature Domains help

Created with Snap316293124155186217248279311342373404435466497528559590181511GH13
Family Start End Evalue family coverage
GH13 181 511 1.5e-123 0.9936708860759493

CDD Domains      download full data without filtering help

Created with Snap316293124155186217248279311342373404435466497528559590128548AmyAc_CMD79578PRK107851546PRK14510181522AmyAc_bac2_AmyA129599AmyA
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11338 AmyAc_CMD 0.0 128 548 1 389
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.
PRK10785 PRK10785 2.86e-99 79 578 75 559
maltodextrin glucosidase; Provisional
PRK14510 PRK14510 6.35e-91 1 546 1 575
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
cd11316 AmyAc_bac2_AmyA 1.52e-55 181 522 20 351
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.
COG0366 AmyA 2.52e-54 129 599 1 505
Glycosidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Created with Snap3162931241551862172482793113423734044354664975285595903619CBL33914.1|GH13_393619CBK97234.1|GH13_394613QNK39367.1|GH13_394613QAT48387.1|GH13_394549QEY35300.1|GH13_39
Hit ID E-Value Query Start Query End Hit Start Hit End
CBL33914.1 5.57e-303 3 619 4 623
CBK97234.1 1.59e-302 3 619 4 623
QNK39367.1 1.47e-201 4 613 1 608
QAT48387.1 1.09e-200 4 613 1 608
QEY35300.1 1.91e-200 4 549 1 548

PDB Hits      download full data without filtering help

Created with Snap3162931241551862172482793113423734044354664975285595901215801BVZ_A1215801JF6_A1215801JF5_A1215801WZM_A1215801JIB_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
1BVZ_A 6.24e-70 121 580 123 538
Alpha-amylaseIi (tvaii) From Thermoactinomyces Vulgaris R-47 [Thermoactinomyces vulgaris],1BVZ_B Alpha-amylase Ii (tvaii) From Thermoactinomyces Vulgaris R-47 [Thermoactinomyces vulgaris],1JI2_A Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2 [Thermoactinomyces vulgaris],1JI2_B Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2 [Thermoactinomyces vulgaris],3A6O_A Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/acarbose complex [Thermoactinomyces vulgaris],3A6O_B Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase 2/acarbose complex [Thermoactinomyces vulgaris]
1JF6_A 6.24e-70 121 580 123 538
ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF6_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1JF5_A 6.24e-70 121 580 123 538
ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF5_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris]
1WZM_A 1.69e-69 121 580 123 538
ChainA, Alpha-amylase II [Thermoactinomyces vulgaris],1WZM_B Chain B, Alpha-amylase II [Thermoactinomyces vulgaris]
1JIB_A 3.27e-69 121 580 123 538
ChainA, NEOPULLULANASE [Thermoactinomyces vulgaris],1JIB_B Chain B, NEOPULLULANASE [Thermoactinomyces vulgaris],1JL8_A Chain A, ALPHA-AMYLASE II [Thermoactinomyces vulgaris],1JL8_B Chain B, ALPHA-AMYLASE II [Thermoactinomyces vulgaris],1VB9_A Chain A, alpha-amylase II [Thermoactinomyces vulgaris],1VB9_B Chain B, alpha-amylase II [Thermoactinomyces vulgaris],2D2O_A Chain A, Neopullulanase 2 [Thermoactinomyces vulgaris],2D2O_B Chain B, Neopullulanase 2 [Thermoactinomyces vulgaris]

Swiss-Prot Hits      download full data without filtering help

Created with Snap3162931241551862172482793113423734044354664975285595905562sp|P38939|APU_THEP35587sp|P36905|APU_THESA5562sp|P16950|APU_THETY5587sp|P38536|APU_THETU121580sp|Q08751|NEPU2_THEVU
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P38939 9.44e-96 5 562 255 845
Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P36905 2.27e-92 5 587 258 880
Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P16950 3.15e-92 5 562 255 846
Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P38536 3.53e-90 5 587 258 879
Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
Q08751 3.42e-69 121 580 123 538
Neopullulanase 2 OS=Thermoactinomyces vulgaris OX=2026 GN=tvaII 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
1.000066 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003319_00677.