CAZyme Information: PITG_17303-t26_1-p1

Basic Information

• Species: Phytophthora infestans
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora infestans
• CAZyme ID: PITG_17303-t26_1-p1
• CAZy Family: GT31
• CAZyme Description: multicopper oxidase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
401	DS028170|CGC3	44867.88	6.7023

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PinfestansT30-4	19344	403677	1547	17797

• Gene Location: location=DS028170:531889-533204(+)

Full Sequence      

MDGLAGITQCYIPPNATAVYHFEPDKAGSFWWHSQHNTQYPYGLRGPLVEKDIDAEYNVA
DIYHGDPGVPPMWDFILINNRGRYNCTAAATYSFTKCSEDQRLTRFRFKTGKKHLLRVMS
MSALAPFEFSIDGHLLRVIAVDGESLEPSELITNITINIGQRYDLLVEAKNATDTPIGSF
WIRATGLNGLPWTAATGANASDGSISDKELDDQLADRRRLVPALRSGLRYVVLLAVYYCQ
TVGVGMTTAELPVTSIPREIFYGDHVEIVLVNEQNEQHPFHLHGHSPWVVGSRHATLADV
QSNTLRPLKLSGAMFRDVYTVPVCPVGDTDACTGVGYVVLRLEADNPGVWTMHCHIDYDI
HGRREAAATSRRRRLLQQYLERLWQLLHRAAFNTATTVTVP

Enzyme Prediction     

EC	1.10.3.2:77

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	1	360	6.4e-57	0.8212290502793296

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.87e-35	2	361	71	514	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.
225043	SufI	8.70e-34	1	358	99	436	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].
259868	CuRO_2_LCC_like	6.72e-29	65	199	23	146	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.
177843	PLN02191	4.99e-28	2	361	93	537	L-ascorbate oxidase
259947	CuRO_2_MaLCC_like	6.19e-28	68	200	25	143	The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces. The subfamily of fungal laccases includes Ma-LCC and similar proteins. Ma-LCC is a multicopper oxidase (MCO) from Melanocarpus albomyces. Its crystal structure contains all four coppers at the mono- and trinuclear copper centers. Laccase is a blue multi-copper enzyme that 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 in fungi and plants. Laccase 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AFY09916.1|AA1	2.61e-127	1	360	94	513
UIZ26488.1|AA1	1.38e-122	1	360	85	505
AFY09915.1|AA1	7.46e-103	1	358	92	531
UIZ26495.1|AA1	5.57e-102	1	358	94	527
AIG56347.1|AA1_2	7.88e-48	2	360	111	526

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HFU_A	1.20e-37	2	360	77	458	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	1.21e-37	2	360	77	458	Chain A, Laccase [Coprinopsis cinerea]
1V10_A	3.12e-34	1	360	97	479	Chain A, Laccase [Rigidoporus microporus]
3PXL_A	8.72e-34	2	362	77	461	Type-2 Cu-depleted fungus laccase from Trametes hirsuta [Trametes hirsuta]
3FPX_A	1.20e-33	2	362	77	461	Native fungus laccase from Trametes hirsuta [Trametes hirsuta],3V9C_A Type-2 Cu-depleted fungus laccase from Trametes hirsuta at low dose of ionization radiation [Trametes hirsuta]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|E9R598|FETC_ASPFU	4.08e-33	1	358	92	480	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|Q09920|FIO1_SCHPO	6.72e-33	1	358	97	485	Iron transport multicopper oxidase fio1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=fio1 PE=3 SV=1
sp|D0VWU3|LAC1_TRAMX	1.59e-32	2	362	77	461	Laccase OS=Trametes maxima OX=259368 PE=1 SV=1
sp|A0A067XMP2|PTAK_PESFW	1.84e-32	2	360	133	538	Oxydoreductase ptaK OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=ptaK PE=2 SV=2
sp|S8FGV1|LAC2_FOMPI	2.19e-32	2	360	101	491	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
1.000072	0.000006

TMHMM  Annotations     

There is no transmembrane helices in PITG_17303-t26_1-p1.