CAZyme Information: An02g07770-T-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: An02g07770-T-p1
• CAZy Family: AA7
• CAZyme Description: Putative trehalose phosphorylase with similarity to Neurospora crassa ccg9

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
688	An02_A_niger_CBS_513_88|CGC8	77666.31	5.8647

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerCBS513-88	14403	425011	346	14057

• Gene Location: location=An02_A_niger_CBS_513_88:1863882-1866234(-)

Full Sequence      

MTTDGIQPFQRRSSFHQLQLSHQFDKNSWEAPPSKTIYAGLSVLFDDDGVTVALAIRDTT
YLLDFHQKDIVPQGGRTVCAEITDYVLNQLREYSDERLEKFIGLAMPTSVVRRCSTLCSR
LWSELDVIPLVLPEESNIGVDHYVDHPVRKSTGWELKSIDEQAESMGRKCVRLFGPENIP
LLQVGFLGLVEVDTAFHVRLTNLEDFQKTVTQRTWDAVNYYADDLKNRGTKIAFFSATPQ
GGGVALMRHALARFSYSLGTDIKWYVPKPRPGVFRITKNNHNILQGVAAPDERLSNEDWD
KVIDWINENAKRYWLSPGGPLRPPEEGGADVIIIDDPQMPALIPIAKKLAPNRPVIFRNH
IQIRSDLIDQPGSPQADTWSWIWKQVQQADLFISHPVSIFVPKDVPNEMVGYMPASTDWL
DGLNKNMREEDVAYYGRVFNSVCRNSGMMTINYPHDEYIVQIARFDPSKGIFDVVDSYEK
FYRRFTSSLPDRSPPKLLICGHGSVDDPDGTVIYDSVLAHIEKDLPDLSDKICVVRLGPS
DQVLNALMSKAKVALQLSTREGFEVKVSEAIHKGTPVIATKAGGIPLQVADKKNGFLVEV
GDTDAVAQHLFDLCTDDDLYERTKKFALEHVCDEVSTVGNALNWLYLSSKLSKKEEVKPH
KQWINDMARSEAGLEYTTKESRLRRISL

Enzyme Prediction     

EC	2.4.1.231:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	454	622	3.1e-34	0.9375

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340823	GT4_trehalose_phosphorylase	6.45e-175	231	651	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	1.00e-23	231	636	4	362	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
395425	Glycos_transf_1	4.68e-21	456	630	2	158	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.
340831	GT4_PimA-like	2.74e-19	454	638	190	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.
340859	GT4_BshA-like	5.19e-17	454	629	194	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK37740.1|GT4	0.0	1	688	1	688
BCS06233.1|GT4	0.0	1	688	1	688
BCR93600.1|GT4	0.0	1	688	1	688
QRD82654.1|GT4	0.0	1	683	1	684
QMW40252.1|GT4	0.0	1	683	1	684

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2X6Q_A	3.53e-41	203	598	16	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	2.31e-40	203	598	16	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	3.15e-40	203	598	16	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	2.34e-27	203	631	2	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]
5D00_A	3.32e-11	454	637	199	361	Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D00_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D01_A Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168],5D01_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A6YRN9|TREPH_PLEPU	4.74e-211	52	688	60	735	Trehalose phosphorylase OS=Pleurotus pulmonarius OX=28995 GN=TP PE=2 SV=1
sp|O75003|TREPH_GRIFR	6.55e-204	37	685	39	725	Trehalose phosphorylase OS=Grifola frondosa OX=5627 PE=1 SV=1
sp|Q9UV63|TREPH_PLESA	9.71e-203	52	688	60	747	Trehalose phosphorylase OS=Pleurotus sajor-caju OX=50053 GN=TP PE=1 SV=1
sp|Q7LYW5|TRET_THELN	7.97e-43	203	631	14	392	Trehalose synthase OS=Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C) OX=523849 GN=treT PE=1 SV=1
sp|Q9HH00|TRET_PYRFU	7.97e-43	203	631	14	392	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
1.000079	0.000000

TMHMM  Annotations     

There is no transmembrane helices in An02g07770-T-p1.