CAZyme Information: MGYG000001913_00006

Basic Information

• Species: UMGS731 sp900544985
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-272; UMGS731; UMGS731 sp900544985
• CAZyme ID: MGYG000001913_00006
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
644	MGYG000001913_1|CGC1	73741.87	4.6214

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001913	2038964	MAG	Denmark	Europe

• Gene Location: Start: 8383; End: 10317 Strand: +

Full Sequence      

MSGFIKGAKIWNRIESKHIVASDNTESAAIFCGAFPADVSVKFSLGKNITAERVSLFLLC
DKSGDSAEYPLSRGKDGVFSVTLSMEEISSAGSLFFYKYEIYNSYGTFYLLHDPEDFSDK
IYENENDGEYFQLLIYKKREKYPDFFRGGIVYQIFPDRFFRGGNEPAAPWAVMNNDWYGG
KVAYCENGDENFKNNMFFGGDLCGIEKKLSYIASLGVTTIYLNPIFVSSSNHKYDTADYL
HVDPMFGGDEAFLSLLKSAKEYGINIILDGVFNHTGDDSIYFNKYGNYDSVGAFQSEESP
YYDWYNFYSFPEKYESWWDFSNLPRVRSDNSAYREFLFGKDGVIRKYIREGICGWRIDVA
DELSDDFLEGLSSAAREEKSDAIVIGEVWEDASNKIAYSKRRSYFSGKELDSVMNYPMRN
AIIDYVRNGDYKRFLLTSNTLYYNYPREVTNVLFNVLGTHDTKRIITALAGADSDGLSKK
ELSEKIMTSEEYSLGVMRLKLAYFILSFIPGVPCIYCGDEIGMEGEDDPFNRRPYPWGME
NTELLGFYRKTGAVRRKEKMLEDADFEVAFADEELLVFERKKSGETLVCIVNRSDRNFKF
TCDKNAFDVFEEKTGEKFCIGPLSCACFKINSEIKYGITVEYEK

Enzyme Prediction     

No EC number prediction in MGYG000001913_00006.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	200	529	2.8e-120	0.9936708860759493

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11338	AmyAc_CMD	1.31e-171	148	566	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	7.73e-97	150	595	123	560	maltodextrin glucosidase; Provisional
PRK14510	PRK14510	8.51e-70	56	596	26	623	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
COG0366	AmyA	6.71e-53	149	605	1	495	Glycosidase [Carbohydrate transport and metabolism].
pfam00128	Alpha-amylase	9.59e-52	200	529	1	334	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAB1243760.1	8.20e-158	94	600	78	583
QNK39367.1	3.77e-153	94	594	78	574
QQR32000.1	3.97e-152	131	635	109	629
ANU56099.1	3.97e-152	131	635	109	629
ASB42775.1	3.97e-152	131	635	109	629

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1J0H_A	3.98e-70	143	618	129	564	Crystalstructure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0H_B Crystal structure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0I_A Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus],1J0I_B Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus]
1SMA_A	1.07e-69	143	618	129	564	CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]
1J0J_A	1.07e-69	143	618	129	564	ChainA, neopullulanase [Geobacillus stearothermophilus],1J0J_B Chain B, neopullulanase [Geobacillus stearothermophilus],1J0K_A Chain A, neopullulanase [Geobacillus stearothermophilus],1J0K_B Chain B, neopullulanase [Geobacillus stearothermophilus]
5BN7_A	1.94e-69	143	595	119	563	Crystalstructure of maltodextrin glucosidase from E.coli at 3.7 A resolution [Escherichia coli K-12]
1GVI_A	1.50e-68	143	618	129	564	Thermusmaltogenic amylase in complex with beta-CD [Thermus sp.],1GVI_B Thermus maltogenic amylase in complex with beta-CD [Thermus sp.]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P38939	1.40e-88	131	581	368	846	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P16950	1.87e-88	125	581	362	847	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P36905	5.66e-88	131	607	371	884	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38536	1.45e-85	131	581	371	846	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P29964	1.15e-69	143	596	126	535	Cyclomaltodextrinase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=Teth39_0676 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000058	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001913_00006.