CAZyme Information: MGYG000002900_01889

Basic Information

• Species: Actinomyces urogenitalis
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Actinomyces; Actinomyces urogenitalis
• CAZyme ID: MGYG000002900_01889
• CAZy Family: GT4
• CAZyme Description: Trehalose synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
476		50598.86	4.4582

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002900	2460697	MAG	United States	North America

• Gene Location: Start: 4319; End: 5749 Strand: +

Full Sequence      

MRSIDVAPLPLSDLESHLDEVAIRRLHDGVAAAHGLLDGRTVWTVTPSAAAEAGPAQTVA
PLVGYARGLGIDARWLTLDAPAEFLAVTARLNAALHGSHGDGGKLADKQRDLYEHVLASN
AENVVEDVREGDVVILHDPATAGLSRAFSQAGATVIWRCHVGATDAGEEGQRAWAFLDRY
LEDADLLVASRAEYLPPYAEEERCAVVAPSINPDSPKNRVLDMDEAASVVRLTGFFDGQP
PFDAVPFIREDGRPDAFRGLGDDAPSAPAAGTPVPEGTRVVTQVQRWDPLKGGLELVEAF
ASQIETLPSDAHLVLAGPTPDPAREPGAARTLEEITERVSTLPESVACRIHVLAIPASDR
EVNATIVNALQRVSAVVTQRSRVEAFGLTVAEAMWKKAAVVGSAVGGIQDQIEDGVSGVL
VAADDAAGWAEAVRDLLLLSERAREMGEVAHEAVRRDYLPDRHLIEVLNVIAQAAV

Enzyme Prediction     

No EC number prediction in MGYG000002900_01889.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	275	448	5e-23	0.9625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03792	GT4_trehalose_phosphorylase	1.36e-62	54	472	13	376	trehalose phosphorylase and similar proteins. Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.
cd03800	GT4_sucrose_synthase	6.13e-22	263	463	205	392	sucrose-phosphate synthase and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
cd03801	GT4_PimA-like	3.75e-21	62	471	23	365	phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
COG0438	RfaB	2.66e-20	276	474	197	377	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
pfam00534	Glycos_transf_1	1.30e-15	277	448	1	153	Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALC98419.1	2.07e-265	1	475	1	474
AMD87259.1	4.68e-257	1	474	1	471
QPL05182.1	9.44e-257	1	474	1	472
VEG28211.1	7.57e-236	1	474	1	470
BDA64638.1	8.49e-234	1	473	1	470

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2X6Q_A	3.79e-46	11	471	16	411	Crystalstructure of trehalose synthase TreT from P.horikoshi [Pyrococcus horikoshii],2X6Q_B Crystal structure of trehalose synthase TreT from P.horikoshi [Pyrococcus horikoshii],2X6R_A Crystal structure of trehalose synthase TreT from P.horikoshi produced by soaking in trehalose [Pyrococcus horikoshii],2X6R_B Crystal structure of trehalose synthase TreT from P.horikoshi produced by soaking in trehalose [Pyrococcus horikoshii]
2XA2_A	2.73e-45	11	471	16	411	Crystalstructure of trehalose synthase TreT mutant E326A from P. horikoshii in complex with UDPG [Pyrococcus horikoshii],2XA2_B Crystal structure of trehalose synthase TreT mutant E326A from P. horikoshii in complex with UDPG [Pyrococcus horikoshii],2XA9_A Crystal structure of trehalose synthase TreT mutant E326A from P. horikoshii in complex with UDPG [Pyrococcus horikoshii],2XA9_B Crystal structure of trehalose synthase TreT mutant E326A from P. horikoshii in complex with UDPG [Pyrococcus horikoshii],2XMP_A Crystal structure of trehalose synthase TreT mutant E326A from P. horishiki in complex with UDP [Pyrococcus horikoshii],2XMP_B Crystal structure of trehalose synthase TreT mutant E326A from P. horishiki in complex with UDP [Pyrococcus horikoshii]
2XA1_A	1.41e-43	11	471	16	411	Crystalstructure of trehalose synthase TreT from P.horikoshii (Seleno derivative) [Pyrococcus horikoshii],2XA1_B Crystal structure of trehalose synthase TreT from P.horikoshii (Seleno derivative) [Pyrococcus horikoshii]
6ZJ4_AAA	7.74e-35	48	471	34	392	ChainAAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis],6ZJ7_AAA Chain AAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis 768-20],6ZJH_AAA Chain AAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis 768-20],6ZMZ_AAA Chain AAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis],6ZN1_AAA Chain AAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O58762	2.83e-45	11	471	15	410	Trehalose synthase OS=Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) OX=70601 GN=treT PE=1 SV=2
Q9HH00	5.00e-41	54	471	52	409	Trehalose synthase OS=Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) OX=186497 GN=treT PE=3 SV=1
Q7LYW5	5.00e-41	54	471	52	409	Trehalose synthase OS=Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) OX=523849 GN=treT PE=1 SV=1
Q1ARU5	1.84e-32	54	473	50	412	Trehalose synthase OS=Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1) OX=266117 GN=treT PE=1 SV=1
C6DT68	2.73e-08	224	450	219	421	D-inositol 3-phosphate glycosyltransferase OS=Mycobacterium tuberculosis (strain KZN 1435 / MDR) OX=478434 GN=mshA 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
1.000040	0.000017	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002900_01889.