CAZyme Information: MGYG000001336_00781

Basic Information

• Species: Limosilactobacillus reuteri_E
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; Limosilactobacillus reuteri_E
• CAZyme ID: MGYG000001336_00781
• CAZy Family: GH70
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1807		200290.98	5.6365

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001336	2316838	Isolate	not provided	not provided

• Gene Location: Start: 747745; End: 753168 Strand: -

Full Sequence      

MFDIKLKYFLNIIYSMLFLDLRGGNILEVKKHFKLYKSGKQWITAAVATVALSAGMVLGG
VAHADTTTPADNQSVATTQPVGSQNKATQDSTQGQTAANNVVPDLLQHTLAAATNNNTQN
ASDLNAQKTQQSQSYNHDDNGSYGNFDSVAVDGNQLHVTGWQATNKAAQYGTDNRYLIVV
GHNDQGQQEELGRTKLTSDMIVNRPDVQKAHNVYNAANSGFNANVQLDVNKLQNYRNAIQ
IISRYSKTADGNGFYDGSDYVSQPVTFDKNNYAYLDQMAVVNSKLHVAGWNATNDALGKA
NHYVILYDQTQGRELARVKVNDQSRPDVANAHKDVINANNSGFAADFSLNGVDLTHQLQV
ISRYSDAANGEGNHVDYWFAPQALLQANLTNQGNLDQFNVSKAGEVTVTGWHATDASNIE
RNHFLILFDQTANRQVASIKVDTVARPDVAKVYPNVKSAGQSGFSATFKVKNGELAANHQ
YAIVSRYSAVADGNGDSGNHTDYWSNGVKLNQSAYWLDHLKMTDQGLHISGWVASDNSLS
QPHAFAFVMNNGKEVARQELKLAARPDVANAYPSLYNSAMSGFDTTIKLDNISKLTGNLQ
VLLRFTNNKNGDLDNGQATDQYSKNYATAGHSFDYVKANGNTVQFAGWDATDQAINLPYQ
WMIVLVNGQEAARQLISSDMTDGLAGFDRTDVYKVFPEVANSAMSGFQGTMTIPVAVKNG
DTVQLVHRFADSSTDAEKQYIQSYSPVLTVNNGSAQLGQYALRKFGLQKKDGKDYYYDPT
TGQVRKNFLMQTKDGWEYFDNDTGAGTDALKLQFDKGTVSLDRLFDYGNKAYDFTSKSIE
NVNGYLTADTWYRPAKILANGTTWTDSKDTDYRPLLMSWWPNKQIQVDYLNYMKKQGYVS
NSQDYTVNDGDYTLNYAAEDIQRNFEKRIAQNGTDWLKQLINDFIKTEPIWNEKTENVNY
SGLQFQGGFLKYENSKLTPYANSDYRLLGRMPINIDGKGYKGAEFLLANDVDNSNPVVQA
EQLNWLYYLLNFGTITGNNDQANFDSVRVDAPDNIDADLMNIAKDYFNAAYGMNSDAVSN
KHINILEDWNSSDPNYFNKIGNPQLTMDVSLKGALNHGLSDSKNRWGLNAIVYQSLANRA
NDSTENEVIPNYSFIRAHDNNSQDQIQNAIRDLTGKDYHTFTQADEKKGIDAYIKDQNST
VKKYNLYNIPSSYAILLTNKDTIPRVYYGDLYTDGGQYMEHRTRYYDTLTNLLKSRVKYV
SGGQSMQTMSIGGNNNVLTSVRYGKGAMKATDSGTAETRTQGIGVVVSNDQNLKLGANDT
VVLHMGAAHKNQEYRAAVLTTDNGVVNYTSDQNAPVAYTNANGDLYLFGRNLIINGQEEA
NTAVKGYANPDVSGYLAVWVPVGASDNQDARTAPSTEKNDGKSAYRSNAAFDSNVIFEAF
SNFVYTPTKESERANVRIAQNADFFASLGFTSFEMAPQYNSSKARTFLDSTIDNGYAFTD
RYDLGMSAPNKYGTDADLRNAIQALHKAGLQVMADWVPDQIYNLPGKEVVTVSRGDDHGN
AWKDSMINNDLYVANTIGGGEYQKKYGGAFLDQLQKLYPELFTKKQVSTGVPIDPSVKIT
EWSAKYFNGTNILHRGSGYVLKADGGQYYNLGTTTKQFLPSQLTGVKAQDNEGFVKGADG
SYYFYNLDGQMVKNTFIQDSTGNWYFFGQDGKMVENQHFVNVDSYGTSGTYFFLNNGVSF
RSGLVQTNDGTYYFDNYGRLVRNQVITVGAMTYTIDQNGKIVKTSYNPDADRPVSTDIGQ
MTDQNRI

Enzyme Prediction     

EC	2.4.1.5	2.4.1.-	2.4.1.140

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH70	875	1675	0	0.9950186799501868

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam02324	Glyco_hydro_70	0.0	875	1675	1	800	Glycosyl hydrolase family 70. Members of this family belong to glycosyl hydrolase family 70 Glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) catalyze the transfer of D-glucopyramnosyl units from sucrose onto acceptor molecules, EC:2.4.1.5. This family roughly corresponds to the N-terminal catalytic domain of the enzyme. Members of this family also contain the Putative cell wall binding domain pfam01473, which corresponds with the C-terminal glucan-binding domain.
NF033840	PspC_relate_1	1.23e-09	1676	1785	513	634	PspC-related protein choline-binding protein 1. Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC.
cd11318	AmyAc_bac_fung_AmyA	1.98e-09	1457	1537	21	100	Alpha amylase catalytic domain found in bacterial and fungal 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 bacterial and fungal proteins. 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.
TIGR03715	KxYKxGKxW	6.92e-08	30	52	1	23	KxYKxGKxW signal peptide. This model describes a novel form of signal peptide that occurs as an N-terminal domain with a recognizable motif, reminiscent of the YSIRK and PEP-CTERM forms of signal peptide. This domain tends to occur on long, low-complexity (usually Serine-rich and heavily glycosylated) proteins of the Firmicutes, and (as with YSIRK) the majority of these proteins have the LPXTG cell wall-anchoring motif at the C-terminus.
cd11314	AmyAc_arch_bac_plant_AmyA	5.53e-07	1457	1537	19	88	Alpha amylase catalytic domain found in archaeal, bacterial, and plant 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 AmyA from bacteria, archaea, water fleas, and plants. 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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEI56976.1	0.0	1	1807	1	1807
AAY86923.1	0.0	27	1807	1	1781
AAX97502.1	0.0	27	1807	1	1781
AAU08015.1	0.0	27	1807	1	1781
CAD19329.1	0.0	27	1807	1	1781

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HZ3_A	0.0	771	1748	4	976	Lactobacillusreuteri N-terminally truncated glucansucrase GTF180(D1025N)-sucrose complex [Limosilactobacillus reuteri]
3KLL_A	0.0	771	1748	4	976	Crystalstructure of Lactobacillus reuteri N-terminally truncated glucansucrase GTF180-maltose complex [Limosilactobacillus reuteri]
3KLK_A	0.0	771	1748	4	976	Crystalstructure of Lactobacillus reuteri N-terminally truncated glucansucrase GTF180 in triclinic apo- form [Limosilactobacillus reuteri],4AYG_A Lactobacillus reuteri N-terminally truncated glucansucrase GTF180 in orthorhombic apo-form [Limosilactobacillus reuteri],4AYG_B Lactobacillus reuteri N-terminally truncated glucansucrase GTF180 in orthorhombic apo-form [Limosilactobacillus reuteri]
4AMC_A	0.0	771	1807	4	1043	Crystalstructure of Lactobacillus reuteri 121 N-terminally truncated glucansucrase GTFA [Limosilactobacillus reuteri]
6SYQ_B	3.73e-302	784	1748	124	1149	ChainB, Alternansucrase [Leuconostoc mesenteroides]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P08987	4.35e-279	712	1696	104	1090	Glucosyltransferase-I OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfB PE=3 SV=3
P49331	5.75e-279	771	1696	178	1119	Glucosyltransferase-S OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfD PE=3 SV=3
P13470	1.15e-270	767	1696	187	1119	Glucosyltransferase-SI OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfC PE=1 SV=2
P27470	1.24e-258	767	1742	154	1125	Glucosyltransferase-I OS=Streptococcus downei OX=1317 PE=3 SV=1
P11001	2.08e-257	767	1742	160	1131	Glucosyltransferase-I OS=Streptococcus downei OX=1317 GN=gtfI 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
0.461027	0.415275	0.114716	0.007951	0.000753	0.000270

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001336_00781.