CAZyme Information: ASPVEDRAFT_81871-t33_1-p1

Basic Information

• Species: Aspergillus versicolor
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
• CAZyme ID: ASPVEDRAFT_81871-t33_1-p1
• CAZy Family: GT21
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
694		77648.70	6.3484

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AversicolorCBS583.65	13364	1036611	142	13222

• Gene Location: location=KV878127:1948077-1950363(-)

Full Sequence      

MADGSIAPGRRASVQQKRRLSTECHPNSWGNAIAGTIYGGLSAVFEKDKVIFAVAIRDAT
YLVDFAQEELPLQSDGNLDKQIGDHMMGHLHKWCDAHLEKIIGLAIPQQLADKCPTVCSR
LWLDLDIIPLVLSDDSKLSLGGEELRYEFQKSMDWELRTLDEQAESMARKCVRLFGPEGI
PLLQVGLSGLVQVDTGFHVQLTNRKNYEESVTSSTWKAIEHYANDLKKRKIKIAFFSATP
QGGGVALMRHAMVRFSHALGTDMKWYVPKPRPGVFRITKTNHNILQGVSAPEERLSKENW
EQVTSWIQENTDRYWLRSGGPLVHPKEGGADVIIIDDPQMPSLIPLAKQSAPSRPVIFRS
HIQIRSDLVAQKGSPQEECWGRMWETIQQADLFVSHPVKTFVPHTVPPETVAYMPASTDW
LDGLNKSMREEDVAYYGRVFNSMVRNSGMPVIDYPADEYIVQVARFDPSKGIPDVVESYE
KFYERMRKSAPDRVPPKLLICGHGSVDDPDGSIIYDSVVTHIESSIPQLADQICIVRLGP
SDQVLNAVMSKAKVALQLSTREGFEVKVSEAIHKGRPVIATKAGGIPLQVIDKGNGFLVD
VGDTDAVANHLFDLCTDDSLWNKMHKFALAHVCDEVSTVGNSLNWLYVASKLSKGEVIKP
NERWLNDMAREEAGIPYQEGENRLKRELLVYKMD

Enzyme Prediction     

EC	2.4.1.231:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	456	625	3.6e-33	0.94375

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340823	GT4_trehalose_phosphorylase	1.39e-172	232	652	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.
223515	RfaB	6.96e-25	229	654	1	372	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
340859	GT4_BshA-like	9.63e-18	455	630	193	348	N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. 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 bacteria, while some of them are also found in Archaea and eukaryotes.
340828	GT4_WlbH-like	2.12e-17	417	608	150	333	Bordetella parapertussis WlbH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.
340831	GT4_PimA-like	6.06e-17	459	639	194	364	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS22533.1|GT4	0.0	1	693	1	693
EAA61099.1|GT4	0.0	1	693	13	666
QRD82654.1|GT4	0.0	1	688	1	688
QMW40252.1|GT4	0.0	1	688	1	688
QMW28182.1|GT4	0.0	1	688	1	688

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2X6Q_A	6.59e-36	205	599	17	363	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	4.15e-35	205	599	17	363	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	7.64e-35	205	599	17	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	8.88e-29	205	632	3	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]
6D9T_A	1.60e-11	455	656	214	400	BshA from Staphylococcus aureus complexed with UDP [Staphylococcus aureus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A6YRN9|TREPH_PLEPU	2.25e-213	11	686	11	732	Trehalose phosphorylase OS=Pleurotus pulmonarius OX=28995 GN=TP PE=2 SV=1
sp|Q9UV63|TREPH_PLESA	2.63e-204	11	686	11	744	Trehalose phosphorylase OS=Pleurotus sajor-caju OX=50053 GN=TP PE=1 SV=1
sp|O75003|TREPH_GRIFR	1.47e-201	17	686	16	725	Trehalose phosphorylase OS=Grifola frondosa OX=5627 PE=1 SV=1
sp|Q9HH00|TRET_PYRFU	1.71e-35	205	603	15	366	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	1.71e-35	205	603	15	366	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
1.000049	0.000001

TMHMM  Annotations     

There is no transmembrane helices in ASPVEDRAFT_81871-t33_1-p1.