CAZyme Information: MGYG000001695_01328

Basic Information

• Species: Megasphaera massiliensis
• Lineage: Bacteria; Firmicutes_C; Negativicutes; Veillonellales; Megasphaeraceae; Megasphaera; Megasphaera massiliensis
• CAZyme ID: MGYG000001695_01328
• CAZy Family: GH13
• CAZyme Description: Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1129	MGYG000001695_52|CGC1	128585.95	4.8867

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001695	2661757	Isolate	France	Europe

• Gene Location: Start: 7188; End: 10577 Strand: -

Full Sequence      

MDLRLYHNSHDFYYRSAFGAVPSGSRLILRLGASGQGENCRAEVRLWQSNVGESHLSMTY
EDQAFKAVVPIPDKGCLLWYYFIVSDGDTTRYYGNNYEQLGGEGAVYEAAPPAYQITVYD
KEAHTPDWFKHAIVYQIFPDRFYRSGDGENLWGKEGAVIHSNWYDKPYYCKREGVGDIVY
YDFFGGNIKGIQEKLPYLKELGITAIYLNPIFESSSNHRYGTADYFRVDPMLGTNEEFAA
FCKAAKEAGMAVILDGVFSHTGADSIYFNRFGHYPGVGAYQSKESLYYEWFRFTNYPDEY
ESWWGVSDLPDVEETTPSYMDFIINKKESVLKYWLNQGIRGWRLDVIDELPVPFLRQFYK
TLKEENPDAVLIGEVWEDASNKVSYSEQREYLSGYDIDSAMNYAQRALMVDFVTGAKEAR
RMNDELTRLRENYPPENFYAMLNLISSHDIERILTVLSAAGGTDVEDVETTAKKRLKLLT
TWQMTMPGAPCIYYGDEAGLTGGKDPDNRRTYPWGREDWDILGWTKALTRLRTAHDALQT
GRFIPLYADGDVYAFARLIEGGRDVFGKPAEDGLFIVAMNRNPSALRTISLYTDGLAYGK
FTNALNKRMEPEVTLNSRLTLTLPPLEAVILQAGEAEKKRSGVLLHPTSLPAAVGKGVLG
TAAYRFVDFLKTAGQSVWQILPLMPPLAGDSPYLSESAFAGNESLISLERLCDWGWLKKD
VVADFIAMGKGLPPSEVAAEKARILWNLSHDKDLIISWQPFRDFCEANAYWLDDYALFRS
IRDFFKGRPWTEWPDDIRRHDAAALTRYGKELSATVSHVKFMQYIFDRQWHELRAYAKEN
GITILGDLPMFVAHDSADCWAHQDQFDLDEDGRPVSVAGVPPDYFSADGQLWGNPLYDYD
AMAADGYQWWTDRFRRMKDLFDELRVDHFRGFAAYWAVPQGAPTAKDGAWKEGPGLDLFR
AVYQKLGRLNLVAEDLGVITDDVCALKDALDLPGMKVFQFHLKDRSDGIRAFDTELNCIA
YTGTHDNNTIRGWYEQELSESEQLHIRRMLDLSDDVSPEELVQAVIAYTYRRRAETVIVP
MQDLLALPAEARMNVPGVADGNWQWQMKEGQTTFDLARRLAKLCRKSGR

Enzyme Prediction     

No EC number prediction in MGYG000001695_01328.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH77	645	1120	7.7e-151	0.979757085020243
GH13	186	507	1.5e-137	0.9968354430379747

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam02446	Glyco_hydro_77	0.0	645	1108	1	458	4-alpha-glucanotransferase. These enzymes EC:2.4.1.25 transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or (1,4)-alpha-D-glucan.
PRK14508	PRK14508	0.0	638	1129	4	496	4-alpha-glucanotransferase; Provisional
PRK14510	PRK14510	0.0	3	1129	1	1220	bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
cd11338	AmyAc_CMD	0.0	131	543	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.
PLN02635	PLN02635	8.32e-156	635	1129	24	525	disproportionating enzyme

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVO27863.1	0.0	1	1129	1	1132
CCC74188.1	0.0	1	1129	1	1132
AVO75120.1	0.0	1	1129	1	1132
ALG42395.1	0.0	1	1129	1	1132
AXL20086.1	0.0	1	1129	1	1132

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2X1I_A	1.36e-121	642	1129	8	499	glycosidehydrolase family 77 4-alpha-glucanotransferase from thermus brockianus [Thermus brockianus]
1FP8_A	1.91e-121	642	1120	8	490	StructureOf The Amylomaltase From Thermus Thermophilus Hb8 In Space Group P21212 [Thermus thermophilus],1FP9_A Structure Of Amylomaltase From Thermus Thermophilus Hb8 In Space Group C2 [Thermus thermophilus]
1CWY_A	1.91e-121	642	1120	8	490	CrystalStructure Of Amylomaltase From Thermus Aquaticus, A Glycosyltransferase Catalysing The Production Of Large Cyclic Glucans [Thermus aquaticus],1ESW_A X-Ray Structure Of Acarbose Bound To Amylomaltase From Thermus Aquaticus. Implications For The Synthesis Of Large Cyclic Glucans [Thermus aquaticus]
2OWC_A	7.74e-121	642	1120	11	492	Structureof a covalent intermediate in Thermus thermophilus amylomaltase [Thermus thermophilus],2OWW_A Covalent intermediate in amylomaltase in complex with the acceptor analog 4-deoxyglucose [Thermus thermophilus],2OWX_A THERMUS THERMOPHILUS AMYLOMALTASE AT pH 5.6 [Thermus thermophilus]
1X1N_A	8.18e-120	637	1115	24	505	Structuredetermination and refinement at 1.8 A resolution of Disproportionating Enzyme from Potato [Solanum tuberosum],6LX1_A Potato D-enzyme complexed with Acarbose [Solanum tuberosum],6LX2_A Potato D-enzyme complexed with CA26 [Solanum tuberosum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P36905	2.24e-134	5	657	256	944	Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38939	4.46e-133	5	606	253	894	Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P16950	1.08e-132	2	606	252	895	Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P38536	3.53e-130	5	637	256	925	Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P72785	1.82e-126	637	1129	3	499	4-alpha-glucanotransferase OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=malQ PE=3 SV=1

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
1.000025	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001695_01328.