CAZyme Information: ACLA_097070-t26_1-p1

Basic Information

• Species: Aspergillus clavatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus clavatus
• CAZyme ID: ACLA_097070-t26_1-p1
• CAZy Family: GT62
• CAZyme Description: glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
682		77262.07	6.3161

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AclavatusNRRL1	9428	344612	287	9141

• Gene Location: location=DS027058:544737-546898(+)

Full Sequence      

MTMQVYASSIHQFQRKISQHQKKKWQESQKQGAWFGPTSEEPNQIRYAGITAKKIDEHNL
TIVIAVRDVVYPLDFLEHHFHVPERNLDTSITDFVLEQLRKYSANHTEKFVGACLTTELT
EKCPRLAPRLWLELDVMPLVIPQRDALGGRYEQEAPWETREADEQAEYLAMKCVRLFGPN
NIPLLQVGFRGLVEVDSGFLMHFATLEDYRRTSSEETWVALEHFAARVREKRVRIAIFGA
TPQGGGVALMRHAFLRLSQLLGLDIQWYVPQPRSGVFRITKMNHNIFQGVAKPDDYLSAS
DEETLRKWVSVNSQRSWSTSGGPLDHPSHGGADIVVVDDPQLTDLIPIAKEKAPSRPVIF
RSHIQIRTDLTCTPGTPQARSWDWLWQRAKQADVFVSHPISESIPPTVPKEMVAYSPAST
DLLDGLNKQMEDCDTAYYGRLFNQWCHKTGVPMVNYPDEEYFVQIARFDPSKGILDVLDS
YAKFHDRLTKSMPEAKIPKLVICGHGSVDDPDASVMFDTTMSHIHEEMPQLADKIAVVRA
SPSDQVLNAILSKSKVVLQLSTREGFEIKVSEALHKAKPVIVTRVGGLPYQVTDGETGFV
VDMNDTDRVAECLYNLWTDEELYAKMRTNAPRSLSDNVTTVGLVSSWLYLIWMLFENPSW
RPRNQLLSDLMLKDLGLASGGS

Enzyme Prediction     

EC	2.4.1.231:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	457	626	8.6e-34	0.94375

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340823	GT4_trehalose_phosphorylase	0.0	234	654	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.
340831	GT4_PimA-like	3.00e-22	457	630	190	344	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.
395425	Glycos_transf_1	9.48e-22	458	632	1	157	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	1.47e-21	231	630	1	353	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340816	Glycosyltransferase_GTB-type	1.60e-15	388	601	51	235	glycosyltransferase family 1 and related proteins with GTB topology. 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. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS06233.1|GT4	6.15e-254	10	677	6	674
BCR93600.1|GT4	6.15e-254	10	677	6	674
BCR85749.1|GT4	1.63e-252	33	676	8	652
CAK37740.1|GT4	4.04e-252	10	677	6	674
QSS62430.1|GT4	6.67e-248	3	676	27	699

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2X6Q_A	1.17e-40	206	637	16	397	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	7.66e-40	206	637	16	397	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	2.67e-39	206	637	16	397	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	7.58e-27	206	602	2	345	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	2.01e-11	459	647	211	378	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|A6YRN9|TREPH_PLEPU	3.29e-173	47	676	44	720	Trehalose phosphorylase OS=Pleurotus pulmonarius OX=28995 GN=TP PE=2 SV=1
sp|O75003|TREPH_GRIFR	4.22e-169	47	676	40	713	Trehalose phosphorylase OS=Grifola frondosa OX=5627 PE=1 SV=1
sp|Q9UV63|TREPH_PLESA	4.20e-165	47	676	44	732	Trehalose phosphorylase OS=Pleurotus sajor-caju OX=50053 GN=TP PE=1 SV=1
sp|Q9HH00|TRET_PYRFU	1.29e-41	206	651	14	409	Trehalose synthase OS=Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) OX=186497 GN=treT PE=3 SV=1
sp|Q7LYW5|TRET_THELN	1.29e-41	206	651	14	409	Trehalose synthase OS=Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) OX=523849 GN=treT PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000038	0.000001

TMHMM  Annotations     

There is no transmembrane helices in ACLA_097070-t26_1-p1.