CAZyme Information: GAQ11865.1

Basic Information

• Species: Aspergillus lentulus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus lentulus
• CAZyme ID: GAQ11865.1
• CAZy Family: GT32
• CAZyme Description: glutamate decarboxylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
983		110054.26	5.4095

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AlentulusIFM54703	9916	N/A	259	9657

• Gene Location: location=BCLY01000017:441287-445574(-)

Full Sequence      

MVHISRVQKRPKGHPAREAEVTDYVYGTHFAAQDLPHHEMAEREMPASVAYRLIKDELSL
DGNPLLNLASFVTTYMEDEAQNLMTDAMSKNFIDYEQYPQTANIQNRCINMIADLLHAPT
ADGPDDQDSIGTSTVGSSEGIMLAMLAMKKRWQNRRKAEGKDSTRPNVVMNSAVQVCWEK
AARYFDVEEKYVYCTETRYVIDPEEAVNLVDENTIGICAILGTTYTGQYEDVKAINDLLI
KKKIDCPIHVDAASGGFVAPFVNPALEWDFRLPKVVSINVSGHKYGLVYPGVGWVFWRSA
EYLPKELIFNVNYLGTEQATFTLNFSKGASNIIGQYYQLIRLGRHGYRSIMQNLTRTADH
LAAELEKLNFIIMSDGAGGGLPLVAYRLPSDENRLWDEYALAHVLRQRGWVIPAYTMAPH
SNQLKMMRIVLREDFSMDRCNVLVEDMKMAMKTLEEMDRAMIEQYIRHSGRHSLSGKPDH
PVYPGEKHSLQGKTGKTHAAGGEAYVNTMELWTLLWLLAATRHVQAKAVFAHFMVANAIN
FTQETWTNDIFAAQAAHIDAFALNLGYGLHNYELILNDAFTVAHRNNFKMFLSFDMGQGS
QWPADEIVHVIDTYATGSAYYKHHDDKPLVSTFEGGQSADVWKDVRHNAQSDFFFIPDWS
SLGIEAASSSPVIDGLMSWHAWPTGAHDMNTTLDEEYIAALDGRPYIMPVSPWFYTNLPV
FHKNWAWRGDDLWFDRWQQVLELAPEYVEIITWNDYGESHYIGPMHEDDLGIFAVGDAPF
NYAEGMPHDGWRTFLPYVIDMYKSGGQNASFDKEGVVSWYRLNPGGACMSGKTTPGQLSV
EGTNTTSPRTLMQDRIFYSALLESAADVTVSIGGASKTGSWADTPSGQKGLYHGSVPIDG
MMGEVEVTLSRAGEQIAQMKGEAITTDCRKNHGYNNWNAWVGSAMGEKNVTSGKTSSDDK
ESGSQRSRPAITLLLGLVLLALV

Enzyme Prediction     

No EC number prediction in GAQ11865.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH71	529	919	6.3e-142	0.9946666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
130848	Glu-decarb-GAD	0.0	25	455	2	431	glutamate decarboxylase. This model represents the pyridoxal phosphate-dependent glutamate (alpha) decarboxylase found in bacteria (low and hi-GC gram positive, proteobacteria and cyanobacteria), plants, fungi and at least one archaon (Methanosarcina). The product of the enzyme is gamma-aminobutyrate (GABA).
397634	Glyco_hydro_71	4.30e-175	529	918	1	372	Glycosyl hydrolase family 71. Family of alpha-1,3-glucanases.
211418	GH71	1.01e-128	523	805	1	283	Glycoside hydrolase family 71. This family of glycoside hydrolases 71 (following the CAZY nomenclature) function as alpha-1,3-glucanases (mutanases, EC 3.2.1.59). They appear to have an endo-hydrolytic mode of enzymatic activity and bacterial members are investigated as candidates for the development of dental caries treatments.The member from fission yeast, endo-alpha-1,3-glucanase Agn1p, plays a vital role in daughter cell separation, while Agn2p has been associated with endolysis of the ascus wall.
223154	GadA	1.79e-118	23	456	21	444	Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism].
99743	DOPA_deC_like	9.84e-91	67	450	1	345	DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD87587.1|GH71	4.10e-181	509	966	1	452
QMW26321.1|GH71	4.24e-181	509	966	2	453
UCK58866.1|GH71	4.59e-180	509	966	1	452
QMW38404.1|GH71	4.75e-180	509	966	2	453
BAE55589.1|GH71	1.16e-174	509	966	1	443

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HBX_A	5.02e-157	14	464	5	454	Crystal structure of GAD1 from Arabidopsis thaliana [Arabidopsis thaliana],3HBX_B Crystal structure of GAD1 from Arabidopsis thaliana [Arabidopsis thaliana],3HBX_C Crystal structure of GAD1 from Arabidopsis thaliana [Arabidopsis thaliana],3HBX_D Crystal structure of GAD1 from Arabidopsis thaliana [Arabidopsis thaliana],3HBX_E Crystal structure of GAD1 from Arabidopsis thaliana [Arabidopsis thaliana],3HBX_F Crystal structure of GAD1 from Arabidopsis thaliana [Arabidopsis thaliana]
5GP4_A	1.65e-125	14	456	8	450	Chain A, Glutamate decarboxylase [Levilactobacillus brevis],5GP4_B Chain B, Glutamate decarboxylase [Levilactobacillus brevis],5GP4_C Chain C, Glutamate decarboxylase [Levilactobacillus brevis]
2DGK_A	1.68e-117	36	456	19	436	Crystal structure of an N-terminal deletion mutant of Escherichia coli GadB in an autoinhibited state (aldamine) [Escherichia coli],2DGK_B Crystal structure of an N-terminal deletion mutant of Escherichia coli GadB in an autoinhibited state (aldamine) [Escherichia coli],2DGK_C Crystal structure of an N-terminal deletion mutant of Escherichia coli GadB in an autoinhibited state (aldamine) [Escherichia coli],2DGK_D Crystal structure of an N-terminal deletion mutant of Escherichia coli GadB in an autoinhibited state (aldamine) [Escherichia coli],2DGK_E Crystal structure of an N-terminal deletion mutant of Escherichia coli GadB in an autoinhibited state (aldamine) [Escherichia coli],2DGK_F Crystal structure of an N-terminal deletion mutant of Escherichia coli GadB in an autoinhibited state (aldamine) [Escherichia coli]
1XEY_A	2.62e-117	36	456	33	450	Crystal structure of the complex of Escherichia coli GADA with glutarate at 2.05 A resolution [Escherichia coli],1XEY_B Crystal structure of the complex of Escherichia coli GADA with glutarate at 2.05 A resolution [Escherichia coli]
1PMM_A	2.62e-117	36	456	33	450	Crystal structure of Escherichia coli GadB (low pH) [Escherichia coli],1PMM_B Crystal structure of Escherichia coli GadB (low pH) [Escherichia coli],1PMM_C Crystal structure of Escherichia coli GadB (low pH) [Escherichia coli],1PMM_D Crystal structure of Escherichia coli GadB (low pH) [Escherichia coli],1PMM_E Crystal structure of Escherichia coli GadB (low pH) [Escherichia coli],1PMM_F Crystal structure of Escherichia coli GadB (low pH) [Escherichia coli],1PMO_A Crystal structure of Escherichia coli GadB (neutral pH) [Escherichia coli],1PMO_B Crystal structure of Escherichia coli GadB (neutral pH) [Escherichia coli],1PMO_C Crystal structure of Escherichia coli GadB (neutral pH) [Escherichia coli],1PMO_D Crystal structure of Escherichia coli GadB (neutral pH) [Escherichia coli],1PMO_E Crystal structure of Escherichia coli GadB (neutral pH) [Escherichia coli],1PMO_F Crystal structure of Escherichia coli GadB (neutral pH) [Escherichia coli],2DGL_A Crystal structure of Escherichia coli GadB in complex with bromide [Escherichia coli],2DGL_B Crystal structure of Escherichia coli GadB in complex with bromide [Escherichia coli],2DGL_C Crystal structure of Escherichia coli GadB in complex with bromide [Escherichia coli],2DGL_D Crystal structure of Escherichia coli GadB in complex with bromide [Escherichia coli],2DGL_E Crystal structure of Escherichia coli GadB in complex with bromide [Escherichia coli],2DGL_F Crystal structure of Escherichia coli GadB in complex with bromide [Escherichia coli],2DGM_A Crystal structure of Escherichia coli GadB in complex with iodide [Escherichia coli],2DGM_B Crystal structure of Escherichia coli GadB in complex with iodide [Escherichia coli],2DGM_C Crystal structure of Escherichia coli GadB in complex with iodide [Escherichia coli],2DGM_D Crystal structure of Escherichia coli GadB in complex with iodide [Escherichia coli],2DGM_E Crystal structure of Escherichia coli GadB in complex with iodide [Escherichia coli],2DGM_F Crystal structure of Escherichia coli GadB in complex with iodide [Escherichia coli],3FZ6_A Crystal structure of glutamate decarboxylase beta from Escherichia coli: complex with xenon [Escherichia coli K-12],3FZ6_B Crystal structure of glutamate decarboxylase beta from Escherichia coli: complex with xenon [Escherichia coli K-12],3FZ6_C Crystal structure of glutamate decarboxylase beta from Escherichia coli: complex with xenon [Escherichia coli K-12],3FZ6_D Crystal structure of glutamate decarboxylase beta from Escherichia coli: complex with xenon [Escherichia coli K-12],3FZ6_E Crystal structure of glutamate decarboxylase beta from Escherichia coli: complex with xenon [Escherichia coli K-12],3FZ6_F Crystal structure of glutamate decarboxylase beta from Escherichia coli: complex with xenon [Escherichia coli K-12],3FZ7_A Crystal structure of apo glutamate decarboxylase beta from Escherichia coli [Escherichia coli K-12],3FZ7_B Crystal structure of apo glutamate decarboxylase beta from Escherichia coli [Escherichia coli K-12],3FZ7_C Crystal structure of apo glutamate decarboxylase beta from Escherichia coli [Escherichia coli K-12],3FZ7_D Crystal structure of apo glutamate decarboxylase beta from Escherichia coli [Escherichia coli K-12],3FZ7_E Crystal structure of apo glutamate decarboxylase beta from Escherichia coli [Escherichia coli K-12],3FZ7_F Crystal structure of apo glutamate decarboxylase beta from Escherichia coli [Escherichia coli K-12],3FZ8_A Crystal structure of glutamate decarboxylase beta from Escherichia coli: reduced Schiff base with PLP [Escherichia coli K-12],3FZ8_B Crystal structure of glutamate decarboxylase beta from Escherichia coli: reduced Schiff base with PLP [Escherichia coli K-12],3FZ8_C Crystal structure of glutamate decarboxylase beta from Escherichia coli: reduced Schiff base with PLP [Escherichia coli K-12],3FZ8_D Crystal structure of glutamate decarboxylase beta from Escherichia coli: reduced Schiff base with PLP [Escherichia coli K-12],3FZ8_E Crystal structure of glutamate decarboxylase beta from Escherichia coli: reduced Schiff base with PLP [Escherichia coli K-12],3FZ8_F Crystal structure of glutamate decarboxylase beta from Escherichia coli: reduced Schiff base with PLP [Escherichia coli K-12],7JZH_A Chain A, Glutamate decarboxylase [Escherichia coli],7JZH_B Chain B, Glutamate decarboxylase [Escherichia coli],7JZH_C Chain C, Glutamate decarboxylase [Escherichia coli],7JZH_D Chain D, Glutamate decarboxylase [Escherichia coli],7JZH_E Chain E, Glutamate decarboxylase [Escherichia coli],7JZH_F Chain F, Glutamate decarboxylase [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q07346|DCE_PETHY	5.55e-158	26	458	18	445	Glutamate decarboxylase OS=Petunia hybrida OX=4102 GN=GAD PE=1 SV=1
sp|Q42521|DCE1_ARATH	3.30e-157	14	464	5	454	Glutamate decarboxylase 1 OS=Arabidopsis thaliana OX=3702 GN=GAD1 PE=1 SV=2
sp|Q42472|DCE2_ARATH	1.21e-154	25	458	16	444	Glutamate decarboxylase 2 OS=Arabidopsis thaliana OX=3702 GN=GAD2 PE=1 SV=1
sp|Q9ZPS3|DCE4_ARATH	4.60e-154	26	458	18	445	Glutamate decarboxylase 4 OS=Arabidopsis thaliana OX=3702 GN=GAD4 PE=1 SV=1
sp|P54767|DCE_SOLLC	2.96e-151	26	458	19	446	Glutamate decarboxylase OS=Solanum lycopersicum OX=4081 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000054	0.000000

TMHMM  Annotations     

There is no transmembrane helices in GAQ11865.1.