CAZyme Information: MGYG000001537_03326

Basic Information

• Species: Cellulomonas timonensis
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Cellulomonadaceae; Cellulomonas; Cellulomonas timonensis
• CAZyme ID: MGYG000001537_03326
• CAZy Family: GH13
• CAZyme Description: Sucrose phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
511	MGYG000001537_13|CGC6	56114.31	5.8655

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001537	4057828	Isolate	not provided	not provided

• Gene Location: Start: 650674; End: 652209 Strand: +

Full Sequence      

MGPASSPRSRLGRGVQLIVYPNRFGATLAGLQRLLDGPILRDVFTGVHLLPFYVPFDGAD
GGFDPIDHTQVDPRLGDWDDVRALADRYSLVADVIVNHMSSAAPQFLDVMERGDDAEHPG
MFLMMGDVFTRGATEEDLLRIFRPRPGPPFTVVPWGARRRLAWTTFTADQIDLDHSDPET
QAYLERVLQALARAGVRMVRLDAAGYAVKTAGTTCFLTPATFEFIRRLTGRAHELGMEVL
VEAHTHYAKQVALASTADWVYDFALPPLVLYSLYTGDGDPLRRWLGVRPSNSVTVLDTHD
GIGVMDIGPSQLDGHQPGLLAVEQIDRIVEGIHEHTDQESRASTGAGASNVDAYQVNTTY
YEAVGRDDQRYLLARALQFFIPGLPQVYYVGLLAGHNDLALLAQTGVGRDINRRKFLTSD
LEEHLARPVVAALFELIRFRNAHPAFDGEFSHAGAPGVIQMTWAHGGHRATLTANLMAGR
ASVAWTDAQGRQRHTPDLLEPDWHSAGGTSA

Enzyme Prediction     

EC	2.4.1.7

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	44	389	4.1e-105	0.9970845481049563

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11355	AmyAc_Sucrose_phosphorylase	0.0	14	451	3	432	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.
cd11343	AmyAc_Sucrose_phosphorylase-like	0.0	13	451	2	444	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	0.0	14	497	4	486	sucrose phosphorylase; Provisional
TIGR03852	sucrose_gtfA	1.29e-131	15	476	3	460	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.
cd11356	AmyAc_Sucrose_phosphorylase-like_1	2.16e-91	17	446	8	442	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
QHT58253.1	4.58e-196	15	499	5	493
QYN21495.1	5.14e-190	16	483	8	474
QZN87677.1	4.18e-188	14	486	4	475
QCP10439.1	8.69e-188	15	484	5	476
BAK33205.1	6.58e-187	15	486	13	484

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1R7A_A	1.96e-167	15	501	5	500	SucrosePhosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis],1R7A_B Sucrose Phosphorylase from Bifidobacterium adolescentis [Bifidobacterium adolescentis]
2GDV_A	3.94e-167	15	501	5	500	Sucrosephosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis],2GDV_B Sucrose phosphorylase from BIFIDOBACTERIUM ADOLESCENTIS reacted with sucrose [Bifidobacterium adolescentis]
2GDU_A	5.58e-167	15	501	5	500	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]
5MB2_B	6.39e-166	15	501	5	500	Structureof sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose [Bifidobacterium adolescentis]
6FME_A	6.84e-166	15	501	6	501	Structureof sucrose phosphorylase from Bifidobacterium adolescentis bound to glycosylated resveratrol [Bifidobacterium adolescentis ATCC 15703],6FME_B Structure of sucrose phosphorylase from Bifidobacterium adolescentis bound to glycosylated resveratrol [Bifidobacterium adolescentis ATCC 15703]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0ZZH6	2.16e-166	15	501	5	500	Sucrose phosphorylase OS=Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) OX=367928 GN=sucP PE=1 SV=1
P33910	9.41e-164	15	483	5	473	Sucrose phosphorylase OS=Agrobacterium vitis OX=373 PE=3 SV=1
E4PMA5	8.81e-104	11	494	3	477	Glucosylglycerol phosphorylase OS=Marinobacter adhaerens (strain DSM 23420 / HP15) OX=225937 GN=gtfA PE=1 SV=1
D9TT09	4.38e-93	15	492	7	483	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
P10249	7.85e-92	17	447	9	430	Sucrose phosphorylase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=gtfA PE=1 SV=4

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
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001537_03326.