CAZyme Information: GLOIN_2v1472570-t44_1-p1

Basic Information

• Species: Rhizophagus irregularis
• Lineage: Mucoromycota; Glomeromycetes; ; Glomeraceae; Rhizophagus; Rhizophagus irregularis
• CAZyme ID: GLOIN_2v1472570-t44_1-p1
• CAZy Family: AA5
• CAZyme Description: multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
289	AUPC02000027|CGC2	32945.50	8.6618

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RirregularisDAOM181602	26245	747089	102	26143

• Gene Location: location=AUPC02000027:157400-158574(-)

Full Sequence      

MVLKELFGGFNGQYPAPIIRANQGDRMIINVENRFGDPAAVHWHGMLQHGTNWYDGVPGQ
TQCPIPNDVSFIYNFTTGDQHGTFWYHSHFMAQYADGLRGALIVHVPDDPYLKEYDYEYV
ITLSDWHHRTTGEILPNFISPTYTGRRPVPDSPLLSGRSRYNCNGVPDGSKCKPNAPLAV
YNVKKNKKYRFRIINTAADAFFIFSIDEYKLKLIESEGIYIKPTIIEKLPINVGQRYSII
VNADQLIGKYWIRATIDKRCALINNATINFNSSIDWNSLGILKYEGSKK

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	10	288	2.6e-86	0.7094972067039106

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	8.22e-57	9	271	24	296	L-ascorbate oxidase, plant type. Members of this protein family are the copper-containing enzyme L-ascorbate oxidase (EC 1.10.3.3), also called ascorbase. This family is found in flowering plants, and shows greater sequence similarity to a family of laccases (EC 1.10.3.2) from plants than to other known ascorbate oxidases.
259926	CuRO_1_Diphenol_Ox	1.69e-50	11	105	25	119	The first cupredoxin domain of fungal laccase, diphenol oxidase. Diphenol oxidase belongs to the laccase family. It catalyzes the initial steps in melanin biosynthesis from diphenols. Melanin is one of the virulence factors of infectious fungi. In the pathogenesis of C. neoformans, melanin pigments have been shown to protect the fungal cells from oxidative and microbicidal activities of host defense systems. Laccase is a blue multicopper oxidase (MCO) which catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
215324	PLN02604	8.25e-50	4	271	42	317	oxidoreductase
259920	CuRO_1_Fet3p	7.04e-49	9	105	24	121	The first Cupredoxin domain of multicopper oxidase Fet3P. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) and a four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the exocellular space and the carboxyl terminus in the cytoplasm. The periplamic produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The four copper ions are inserted post-translationally and are essential for catalytic activity, thus linking copper and iron homeostasis. Like other related multicopper oxidases (MCOs), Fet3p is composed of three cupredoxin domains that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
177843	PLN02191	1.45e-48	11	259	48	307	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX53525.1|AA1	3.21e-78	2	284	123	402
AGY56171.2|AA1_1	3.17e-69	11	287	46	301
CDJ79884.1|AA1_1|1.10.3.2	2.55e-68	11	254	56	289
QPA20094.1|AA1_1	1.25e-66	12	257	50	287
AUS45844.1|AA1	3.60e-66	11	287	147	422

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4JHU_A	1.27e-63	11	287	28	283	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
3KW7_A	2.86e-63	11	287	28	284	Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2],3KW7_B Crystal structure of LacB from Trametes sp. AH28-2 [Trametes sp. AH28-2]
6H5Y_A	1.93e-62	11	287	28	283	PM1 mutant, 7D5 [Aspergillus oryzae],6H5Y_B PM1 mutant, 7D5 [Aspergillus oryzae]
2HRG_A	3.81e-62	11	287	28	283	Crystal Structure of Blue Laccase from Trametes trogii complexed with p-methylbenzoate [Coriolopsis trogii],2HRH_A Crystal Structure of Blue Laccase from Trametes trogii [Coriolopsis trogii]
1GYC_A	6.14e-61	11	287	28	284	Chain A, LACCASE 2 [Trametes versicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q12739|LAC2_PLEOS	8.42e-61	15	254	66	294	Laccase-2 OS=Pleurotus ostreatus OX=5322 GN=POX2 PE=1 SV=1
sp|Q01679|LAC1_PHLRA	1.27e-60	12	254	50	283	Laccase OS=Phlebia radiata OX=5308 GN=LAC PE=1 SV=2
sp|Q12718|LAC2_TRAVE	6.75e-60	11	287	48	304	Laccase-2 OS=Trametes versicolor OX=5325 GN=LCC2 PE=1 SV=1
sp|Q99046|LAC2_TRAVI	1.01e-58	11	287	48	304	Laccase-2 OS=Trametes villosa OX=47662 GN=LCC2 PE=3 SV=1
sp|S8FGV1|LAC2_FOMPI	1.26e-58	11	254	52	285	Laccase-2 OS=Fomitopsis pinicola (strain FP-58527) OX=743788 GN=LCC2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000029	0.000007

TMHMM  Annotations     

There is no transmembrane helices in GLOIN_2v1472570-t44_1-p1.