CAZyme Information: PIS53400.1

Basic Information

• Species: [Candida] auris
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; [Candida] auris
• CAZyme ID: PIS53400.1
• CAZy Family: GH65
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
641		72816.05	4.6688

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CaurisB11221	5715	N/A	194	5521

• Gene Location: location=PGLS01000004:1967483-1969408(-)

Full Sequence      

MNLLTLYFFWLIPLTVHALSKTHEFHFNASLIKKNPDGVRERDVIAINGQWPLPIIRVTR
HDRVIIHLTNEMPDRNTSLHFHGLFMNGTNAMDGPEHVTQCPIPPGHTFTYNFTVDDQAG
TYWYHSHSGSQYSDGLRGMFIIEEESRDLYPFTFDEEVPLTVCDWYHAQSSDIMSQFLSR
YNPTGAEPIPQNSLFNDTRNVTWNVEPDKTYFLRIVNMGMFVSQYLYIENHTFTIVEVDG
VYVEPVETESLYITVAQRYGVLLKTKKDVGNEVFRFVNVLDEPMLDLIPDDLQIISTNYL
QYGRGRPDKPAPLANGKGKFDKLVQFLDPYDDIKLVPASKRPLYEDFDVQIVLNFTMDNL
GDGVNYAFFNDITYTAPKVPTLFSVLSAGKFANNAAIYGSNTNTHVLQPGEVVEIVLNNM
DSGKHPFHLHGHVFQTVFRSEGTDDDDNPEVYDPSNSDYEIFPKMPMQRDTVLVNPNGFI
RIRFKADNPGVWFFHCHVDWHLEQGLAIVLVEDPASIQKKQAELPLSHLEACEKLNIPTK
GNAAARFGDTEESWLDLTGENLQVKPLPPGFTPKGYVAIVACALAAVYGIYTIYIYGMED
VNTENAEHMVQKLYQLLGESGDGESEERVRLNSATPLNENE

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	41	390	4.4e-148	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
274555	ascorbase	3.96e-87	22	512	1	523	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	9.93e-87	46	515	56	451	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	1.73e-79	348	514	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.
177843	PLN02191	1.53e-75	9	519	6	553	L-ascorbate oxidase
259945	CuRO_2_Fet3p_like	3.28e-73	156	303	1	147	The second 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 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
QEL59042.1|AA1_2	0.0	1	641	1	641
QEO20037.1|AA1_2	0.0	1	641	1	641
QRG36491.1|AA1_2	0.0	1	641	1	641
QWW22201.1|AA1_2	0.0	16	619	2099	2702
QWU86473.1|AA1_2	0.0	8	632	5	629

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	6.44e-200	21	570	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]
2XYB_A	3.07e-74	35	513	16	468	CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS [Trametes cinnabarina]
3KW7_A	1.33e-73	36	513	17	473	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]
1GYC_A	1.28e-72	29	518	6	475	Chain A, LACCASE 2 [Trametes versicolor]
2QT6_A	4.91e-71	28	513	12	469	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|P78591|FET3_CANAX	7.46e-226	20	601	21	582	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|Q96WT3|FET3_CANGA	1.98e-213	22	601	19	586	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|Q6CII3|FET3_KLULA	2.80e-212	18	607	23	597	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|P38993|FET3_YEAST	7.05e-209	18	614	19	598	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|I1RMG9|FET3_GIBZE	1.72e-203	18	597	20	576	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000372	0.999637	CS pos: 18-19. Pr: 0.9811

TMHMM  Annotations     

Start	End
575	597