CAZyme Information: AWU75157.1

Basic Information

• Species: Pichia kudriavzevii
• Lineage: Ascomycota; Saccharomycetes; ; Pichiaceae; Pichia; Pichia kudriavzevii
• CAZyme ID: AWU75157.1
• CAZy Family: GH47
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
632	CP028774|CGC6	71699.26	4.4985

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PkudriavzeviiCBS573	5367	N/A	212	5155

• Gene Location: location=CP028774:832864-834762(-)

Full Sequence      

MLVLWYLYLCFATAFASEVHEFYFNVEYVNANPDGVFERQVISFNGSWPLPTIEVSRGDR
VKVHLTNSLEDTTTSLHFHGLKMKGKVHMDGPVGVTQCPISPGETMLYDFVVEQAGTYWY
HSHSGAQYSDGMRGLLIVHDKELESLYEFDKELSWSISDWYHDSSSVLVKKQLTKYNPTG
GEPVPQNILFNDSRNVTISIDYDTAYLIRIVNVGIMVSQYFSIPGYEFDIIEVDGVYTHP
KTATMAYLAVGQRMSIILKTKSREDVSSNILIFTAMDEDMLDIVPDDLELNSYNYMSYDG
ALPEPKIPNWVTDRESFNPIDDMDLVPMKKKPLFEDPDHRIEVVLHMENLGDGISYAFFN
NVTYVAPKVPTLLTALSAPENLVKDSRIYGSNTNSFILNHDEIVEIVVNNEDDGKHPMHL
HGHQFQVVARSPELEEPSHYNPENQTFPPFPMMRDTVMVEGGGFLVLRFKANNPGVWFFH
CHLDFHLEQGLALTLVEAPDLINITLPDDQLNICKTAGIPTKGNAAGNAEDFLNLEGENV
QPKPLPDGFTAKGYFALFLCTAIALFGLKSIYDFGMHDILQTESEKIQIEKKVIEKYIDL
LEQMKSNDTDEPFEVDQLLQKAINLNERFSKF

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	38	379	1.4e-139	0.9910979228486647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	5.98e-84	44	499	57	450	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].
259966	CuRO_3_Fet3p	2.72e-83	338	499	1	160	The third Cupredoxin domain of multicopper oxidase Fet3p. Fet3p catalyzes the ferroxidase reaction, which couples the oxidation of Fe(II) to Fe(III) with the four-electron reduction of molecular oxygen to water. Fet3p is a type I membrane protein with the amino-terminal oxidase domain in the extracellular space and the carboxyl terminus in the cytoplasm. The periplasmic 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 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
274555	ascorbase	1.34e-78	19	511	1	536	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.
177843	PLN02191	1.77e-72	2	511	3	559	L-ascorbate oxidase
259920	CuRO_1_Fet3p	1.35e-67	20	139	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWU75157.1|AA1_2	0.0	1	632	1	632
AWT08580.1|AA1_2	0.0	1	632	1	632
QOU19549.1|AA1_2	3.53e-255	2	632	7	644
QPG73697.1|AA1_2	5.83e-222	89	598	1	516
ANZ73894.1|AA1_2	2.13e-220	17	585	20	591

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	5.80e-175	18	548	1	534	Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_B Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_C Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_D Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_E Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae],1ZPU_F Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import [Saccharomyces cerevisiae]
1V10_A	5.68e-66	30	506	34	496	Chain A, Laccase [Rigidoporus microporus]
3KW7_A	1.02e-63	30	516	14	493	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]
5NQ7_A	1.05e-63	32	514	37	507	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]
2QT6_A	1.30e-62	30	516	12	489	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6CII3|FET3_KLULA	1.13e-193	12	588	20	600	Iron transport multicopper oxidase FET3 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=FET3 PE=3 SV=1
sp|P43561|FET5_YEAST	2.17e-191	12	585	13	603	Iron transport multicopper oxidase FET5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET5 PE=1 SV=1
sp|P78591|FET3_CANAX	1.51e-189	12	585	16	588	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|Q96WT3|FET3_CANGA	3.20e-186	11	583	11	590	Iron transport multicopper oxidase FET3 OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=FET3 PE=3 SV=1
sp|K7NCS2|FETC_EPIFE	2.17e-183	24	587	27	587	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000361	0.999569	CS pos: 16-17. Pr: 0.9729

TMHMM  Annotations     

There is no transmembrane helices in AWU75157.1.