CAZyme Information: EPrPAT00000021728-p1

Basic Information

• Species: Pythium aphanidermatum
• Lineage: Oomycota; NA; ; Pythiaceae; Pythium; Pythium aphanidermatum
• CAZyme ID: EPrPAT00000021728-p1
• CAZy Family: GT2
• CAZyme Description: Multicopper oxidase.

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
458	PaphDAOMBR444_SC0493|CGC1	51201.75	6.6836

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PaphanidermatumDAOMBR444	12363	1223555	58	12305

• Gene Location: location=PaphDAOMBR444_SC0493:64-1440(+)

Full Sequence      

MLYKFTPSEAGSYWWHSHENTQYVDGLRGPLIILNRPELQQPGEAVDCEYTVELTDWYHQ
QAAVLLRDMMDPIKNPGGNEPVWDTVLINNRGRFDCSKIPLSTTPELPCTNYQPLSRFRF
KRGRRYRFRLINVAAFAAFDFSIDNHEFRVVAADGLLVKTSPLINSIRVNVGMRYDIIVE
ARPQGVGQHMPPRSFWMRATSLFGGPWTSLPINMFPVGFNPNGLAIIDYNEAKGEPMTSP
WIVKKTIGELDVKPLHPAKLPLLPDTRIIAEFTMTSTLENPVTLGYFSINGRPLSTFVMP
DKPTLFEVAKGVPTSSLPSSSNAVAVGFRKLVELVLVNKDAGEHPFHMHGHPTWVLGAGN
MPNAQSTPTGLNLFDPPLRDGYTMPGCTVDAGGSCVDVGYVVLRFRTDNPGVWMLHCHID
WHLATGLAMLIVEAEEELQKQDPSQFKSVEKQTCSGMY

Enzyme Prediction     

No EC number prediction in EPrPAT00000021728-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	2	428	7.7e-65	0.7849162011173184

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	1.05e-44	2	440	88	530	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.
259868	CuRO_2_LCC_like	2.50e-43	50	229	1	152	Cupredoxin domain 2 of laccase-like multicopper oxidases; including laccase, CueO, spore coat protein A, ascorbate oxidase and similar proteins. Laccase-like multicopper oxidases (MCOs) are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. 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 2 of 3-domain MCOs has lost the ability to bind copper.
259953	CuRO_2_MCO_like_1	2.49e-41	50	230	1	163	The second cupredoxin domain of uncharacterized multicopper oxidase. Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This family of MCOs 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 2 of 3-domain MCOs has lost the ability to bind copper.
177843	PLN02191	2.82e-40	3	440	111	553	L-ascorbate oxidase
215324	PLN02604	2.41e-39	3	440	112	553	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ26495.1|AA1	5.53e-131	2	456	112	563
AFY09915.1|AA1	6.74e-127	2	458	110	569
AFY09916.1|AA1	1.11e-119	2	456	112	546
UIZ26488.1|AA1	5.09e-113	2	456	103	538
AIG56347.1|AA1_2	7.54e-79	1	456	127	556

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Z1X_A	6.09e-56	1	444	93	476	Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z1X_B Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena],5Z22_A Crystal Structure of Laccase from Cerrena sp. RSD1 [Cerrena]
1V10_A	4.00e-53	1	433	114	489	Chain A, Laccase [Rigidoporus microporus]
5EHF_A	3.59e-51	1	433	93	467	Laccase from Antrodiella faginea [Antrodiella faginea]
6RHH_A	1.91e-49	7	443	101	479	Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RHI_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RHO_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RHP_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twenty first structure of the series with 4415 KGy dose (collected after refreezing). [Steccherinum murashkinskyi],6RHR_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. First structure of the series with 15 KGy dose. [Steccherinum murashkinskyi],6RHU_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Second structure of the series with 165 KGy dose. [Steccherinum murashkinskyi],6RHX_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RI0_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RI2_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RI4_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. First structure of the series with 13 KGy dose. [Steccherinum murashkinskyi],6RI6_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Second structure of the series with 400 KGy dose. [Steccherinum murashkinskyi],6RI8_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Third structure of the series with 800 KGy dose. [Steccherinum murashkinskyi],6RII_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourth structure of the series with 1200 KGy dose. [Steccherinum murashkinskyi],6RIK_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Thirteenth structure of the series with 5200 KGy dose. [Steccherinum murashkinskyi],6RIL_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourteenth structure of the series with 5600 KGy dose (data was collected after refreezing). [Steccherinum murashkinskyi]
5MEJ_A	1.95e-49	7	443	101	479	Structural study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi. First structure of the series with 3 min total X-ray exposition time. [Steccherinum murashkinskyi],5MHU_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The third structure of the series with total exposition time 63 min. [Steccherinum murashkinskyi],5MHV_A The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The fourth structure of the series with total exposition time 93 min. [Steccherinum murashkinskyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|S8FGV1|LAC2_FOMPI	8.44e-57	1	438	117	506	Laccase-2 OS=Fomitopsis pinicola (strain FP-58527) OX=743788 GN=LCC2 PE=1 SV=1
sp|E9R598|FETC_ASPFU	7.06e-52	1	440	109	499	Iron transport multicopper oxidase fetC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fetC PE=2 SV=1
sp|S8FIE4|LAC1_FOMPI	4.00e-51	1	433	117	493	Laccase-1 OS=Fomitopsis pinicola (strain FP-58527) OX=743788 GN=LCC1 PE=1 SV=1
sp|Q02079|LAC3_THACU	1.87e-50	9	439	120	545	Laccase-3 OS=Thanatephorus cucumeris OX=107832 GN=LCC3 PE=2 SV=1
sp|Q12542|LAC2_AGABI	2.05e-50	1	437	111	491	Laccase-2 OS=Agaricus bisporus OX=5341 GN=lcc2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000066	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EPrPAT00000021728-p1.