CAZyme Information: MGYG000002638_00336

Basic Information

• Species: Lachnoanaerobaculum orale
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnoanaerobaculum; Lachnoanaerobaculum orale
• CAZyme ID: MGYG000002638_00336
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
569	MGYG000002638_7|CGC1	65534.93	5.1367

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002638	2571408	MAG	China	Asia

• Gene Location: Start: 35934; End: 37643 Strand: -

Full Sequence      

MKKNNNGPMLNAYPDSLGGSLSDIVNFLGKKELKDVFSSFYILPSLFNTDLDRGFSVIDY
SLNELYAKREDLEKLEELGIDLKLDFILNHASVLSKQFQDIIKNGEKSKYRDFFIDWNKF
WDGCGEMTKEGYIQPDKEYIKDMFFRKPGLPILMVRFPDGKEVPYWNTFYQEVKYPTLDA
VDIRNITGVQYSIADGLANLLNKGLCEGKSPANILNVANIYTDKLSESQKKELCERLESE
RKYLGQMDLNIQSPLVWEFYDNTLKTLANYGAKIVRLDAFAYAPKGVGEKNFLNEPATWD
VLTKVRELADKYNVRLLPEIHASYEEKIYEKIANKGYMTYDFFLPGLIIDAFEQQSGEVL
KKWADELVEKKIQVVNMLGCHDGIPLLDLKGLISEERIQSVIDTVVKRGGYVKDLHGQKN
VYYQVNATYYSALGDDDKRMLLARAIQIFMPGKPQVWYLDLFAGKNDHEAVKRAGAGGHK
EINRTNLTAKEMEDGLQKEIVQKQLELLRLRSTFSVFSNDSEFTMKCDESKIFMEWKNNE
ERAVLKADLADCDFEIFVEKNGEKVYQYK

Enzyme Prediction     

No EC number prediction in MGYG000002638_00336.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	246	458	4.8e-61	0.6588921282798834

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11355	AmyAc_Sucrose_phosphorylase	1.00e-123	6	520	2	430	Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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.
TIGR03852	sucrose_gtfA	1.19e-98	6	556	1	467	sucrose phosphorylase. In the forward direction, this enzyme uses phosphate to cleave sucrose into D-fructose + alpha-D-glucose 1-phosphate. Characterized representatives from Streptococcus mutans and Bifidobacterium adolescentis represent well-separated branches of a molecular phylogenetic tree. In S. mutans, the region including this gene has been associated with neighboring transporter genes and multiple sugar metabolism.
cd11343	AmyAc_Sucrose_phosphorylase-like	1.49e-93	6	523	2	445	Alpha amylase catalytic domain found in sucrose phosphorylase (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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.
PRK13840	PRK13840	8.37e-83	5	563	2	480	sucrose phosphorylase; Provisional
cd11356	AmyAc_Sucrose_phosphorylase-like_1	2.15e-50	9	524	7	449	Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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
AYB00851.1	0.0	1	567	1	567
ADL34994.1	4.39e-282	1	556	1	551
AOZ95686.1	4.55e-282	6	556	7	550
QFJ54635.1	1.03e-279	6	556	3	546
BCJ97061.1	1.53e-277	5	567	10	566

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6S9U_A	2.91e-186	6	562	12	515	Crystalstructure of sucrose 6F-phosphate phosphorylase from Ilumatobacter coccineus [Ilumatobacter coccineus YM16-304]
6S9V_A	4.04e-86	6	565	19	498	Crystalstructure of sucrose 6F-phosphate phosphorylase from Thermoanaerobacter thermosaccharolyticum [Thermoanaerobacterium thermosaccharolyticum DSM 571],6S9V_B Crystal structure of sucrose 6F-phosphate phosphorylase from Thermoanaerobacter thermosaccharolyticum [Thermoanaerobacterium thermosaccharolyticum DSM 571]
1R7A_A	7.13e-50	6	545	3	463	SucrosePhosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis],1R7A_B Sucrose Phosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis]
2GDV_A	1.36e-49	6	545	3	463	Sucrosephosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis],2GDV_B Sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis]
2GDU_A	1.89e-49	6	545	3	463	E232Qmutant of sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS in complex with sucrose [Bifidobacterium adolescentis],2GDU_B E232Q mutant of sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS in complex with sucrose [Bifidobacterium adolescentis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0A6C7EEG6	1.21e-185	6	562	12	515	Sucrose 6(F)-phosphate phosphorylase OS=Ilumatobacter coccineus (strain NBRC 103263 / KCTC 29153 / YM16-304) OX=1313172 GN=YM304_32550 PE=1 SV=1
D9TT09	1.51e-85	6	565	5	484	Sucrose 6(F)-phosphate phosphorylase OS=Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) OX=580327 GN=spp PE=1 SV=1
Q59495	8.83e-75	6	565	5	481	Sucrose phosphorylase OS=Leuconostoc mesenteroides OX=1245 PE=1 SV=1
P10249	7.88e-66	6	565	5	478	Sucrose phosphorylase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfA PE=1 SV=4
E4PMA5	3.61e-56	6	549	5	458	Glucosylglycerol phosphorylase OS=Marinobacter adhaerens (strain DSM 23420 / HP15) OX=225937 GN=gtfA PE=1 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
1.000061	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002638_00336.