CAZyme Information: SMAC_05699-t26_1-p1

Basic Information

• Species: Sordaria macrospora
• Lineage: Ascomycota; Sordariomycetes; ; Sordariaceae; Sordaria; Sordaria macrospora
• CAZyme ID: SMAC_05699-t26_1-p1
• CAZy Family: GH2
• CAZyme Description: trehalose synthase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
894		99533.37	6.5749

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Smacrosporak-hell	11311	771870	484	10827

• Gene Location: location=NW_003546212:330227-333099(-)

Full Sequence      

MSSSGSSSGVDRELEQAENDDSAAAAIDAIAFRDPFADTTPRRPTTDNASSRSGTKSPSP
LNSTGTQGSLHSPPSLGVQQLLSDIQPRDPLYDHNTPAPIHPGSDTLAYNNTSPSEEVLR
SLEHHSSKLPTIPSQLQEQQQLDHAQANTGHYTHPSGDNTQTYGTPSAGHHHHSLKPIAT
VIMGFEKARKFSTGTSVHRKRQMSTLVEKEGHFGPALTTLYLGISAVFSDDHTAVVALAI
HDTIYLVDFSVKHIELDDALKMGEDLIADFVISEVQKYEHENFSKFIGAGLPTTLKYMSP
NLCSRLWLELDIVPIVMRPDDEHKEKTFWDVKRVDEQADSMARKCIMNFGPSLVPLLQVG
FRGIVQIDAGFRAHLTTVQNHKDTCSAATWETTLTYAKKLRANKTKIAFFSSTPQGGGVA
LMRHALVRFARLLGVDLTWYVPKPRPGVFRITKNIHNILQGVSHPDQRVTADEKQAIIDW
INENASRYWFSEGGPLRAPEEGGADIVVIDDPQMPGLIPLIKKYTPDRPVLYRSHIQIRS
DLVAKAGSPQADIWDFLWSNIQGCDMFISHPIPIFVPHNVPREKVVYFPATTDWLDGLNK
HLNHWDSGYYGHLYNVACHSQRMTELNWPARKYIIQVARFDPSKGIPTVIDSYAEFRRRC
DKANITDVPQLVVCGNGSVDDPDASLIYDQTMAQLETYYPDLVRDVSVMRLDPKDQLINT
LLANAHVVLQLSTREGFEVKVSEALHAGRPVIVSNVGGIPLQVKDKVNGFLVAPGDWRAI
AGHLMELFTDEELWKKMSHEARTGVSDEVGTVGNGLGWFYLAAKWTEVGVEKNGRGGLKG
NERWVNDMAREEAGYFYTQGENRLPRHFTQRKPELEAEAKDLPVHDKKKAEVAA

Enzyme Prediction     

EC	2.4.1.231:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	630	798	2.7e-33	0.94375

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340823	GT4_trehalose_phosphorylase	0.0	406	825	1	378	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.
395425	Glycos_transf_1	2.74e-25	631	802	2	156	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.
223515	RfaB	7.89e-25	403	802	1	354	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340831	GT4_PimA-like	1.60e-23	629	802	190	345	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.
340830	GT4_sucrose_synthase	3.41e-21	622	805	210	383	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VBB80726.1|GT4	0.0	130	887	69	825
AEO59616.1|GT4	0.0	183	887	1	697
CAP61931.1|GT4	0.0	130	887	72	853
CDP29006.1|GT4	0.0	130	887	72	853
QBZ63163.1|GT4	0.0	186	870	3	687

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2X6Q_A	2.63e-37	397	805	35	394	Crystal structure 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	1.60e-36	397	805	35	394	Crystal structure 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	2.93e-36	397	772	35	363	Crystal structure 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	1.97e-31	396	805	20	375	Chain AAA, 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]
2JJM_A	2.72e-09	630	808	210	368	Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_B Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_C Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_D Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_E Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_F Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_G Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_H Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_I Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_J Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_K Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_L Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O75003|TREPH_GRIFR	8.26e-224	192	866	9	725	Trehalose phosphorylase OS=Grifola frondosa OX=5627 PE=1 SV=1
sp|A6YRN9|TREPH_PLEPU	1.18e-222	216	866	39	732	Trehalose phosphorylase OS=Pleurotus pulmonarius OX=28995 GN=TP PE=2 SV=1
sp|Q9UV63|TREPH_PLESA	1.65e-214	216	866	39	744	Trehalose phosphorylase OS=Pleurotus sajor-caju OX=50053 GN=TP PE=1 SV=1
sp|O58762|TRET_PYRHO	7.26e-37	397	805	34	393	Trehalose synthase OS=Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) OX=70601 GN=treT PE=1 SV=2
sp|Q9HH00|TRET_PYRFU	2.29e-36	397	772	28	361	Trehalose synthase OS=Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) OX=186497 GN=treT PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000037	0.000003

TMHMM  Annotations     

There is no transmembrane helices in SMAC_05699-t26_1-p1.