CAZyme Information: CPAR2_603590-T-p1

Basic Information

• Species: Candida parapsilosis
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida parapsilosis
• CAZyme ID: CPAR2_603590-T-p1
• CAZy Family: GT39
• CAZyme Description: Has domain(s) with predicted copper ion binding, oxidoreductase activity

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
633		71835.89	4.3837

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CparapsilosisCDC317	5984	578454	147	5837

• Gene Location: location=Contig005504_C_parapsilosis_CDC317:852663-854564(-)

Full Sequence      

MRLWNFLSVLFLSTLIAAETHEWWFKTGWVDGLNPDGVYNRSMIGFNGSWPLPTLRVKKY
DRVVLHLINGFDTANTTLHFHGMFQAGSTQMDGPPFVTQCPIPHGEVYTYNFSVDGQVGS
YWYHSHTSGQYGDGMRGVFIIEEPSKDDYPYDYDEEVVLTLNEHYHKTSDELMPDFLSRF
NPTGAEPIIDNILFNETRNATWKVEPNKTYLLRIINTGRFISQYVWIEDHNMTVVEVDGV
YTEPKEASMLYVTIAQRYTVLITTKNSTDKNYAFMNKADDTMLDTIPGDLQLNGTNYMMY
NDGDKPGQNYVDSIDDFLDDFYLVPLDKQEILDDADYTVTVQVQMDNLGNGINYAFFNNI
SYTAPKVPTILSVLSAGEHATNELVYGSNTNTFVLEEDEVVDIVLNNLDTGTHPFHLHGH
VFQVLERGEARDDDEDPIAFNASDHAEWPKYPMKRDTLYVRPQSYFVIRFKADNPGVWFF
HCHIEWHLDQGLAVVFVENPNAIRNNETQQITDNHKQICEKVGVPWEGNAAGNKENVLDL
KGENLQHKRLPTGFTARGIVALVFSCVAGVLGLAAIAFYGMQDINNVEERVARDLDVDLD
EADESGSHDTVDEIVAEGNSSTHERSSTAKYSN

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	40	378	9.6e-148	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	6.12e-91	10	501	25	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	1.03e-80	336	500	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.
259945	CuRO_2_Fet3p_like	1.50e-77	155	302	1	148	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.
274555	ascorbase	2.42e-77	35	505	15	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.
274556	laccase	9.38e-68	41	497	22	518	laccase, plant. Members of this protein family include the copper-containing enzyme laccase (EC 1.10.3.2), often several from a single plant species, and additional, uncharacterized, closely related plant proteins termed laccase-like multicopper oxidases. This protein family shows considerable sequence similarity to the L-ascorbate oxidase (EC 1.10.3.3) family. Laccases are enzymes of rather broad specificity, and classification of all proteins scoring about the trusted cutoff of this model as laccases may be appropriate.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAX40996.1|AA1_2	0.0	7	622	9	613
AOW29995.1|AA1_2	0.0	11	596	14	596
CAX40995.1|AA1_2	0.0	7	600	10	600
AOW29996.1|AA1_2	0.0	7	622	9	613
CAX40994.1|AA1_2	0.0	9	597	12	595

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.78e-242	19	553	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]
3KW7_A	1.84e-68	33	499	15	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]
1V10_A	5.93e-64	33	521	35	510	Chain A, Laccase [Rigidoporus microporus]
2QT6_A	6.86e-63	35	514	17	485	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
1GYC_A	9.81e-62	33	504	15	475	Chain A, LACCASE 2 [Trametes versicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P78591|FET3_CANAX	0.0	11	596	14	594	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|Q6CII3|FET3_KLULA	3.76e-270	13	600	20	607	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	8.68e-263	7	605	8	611	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|Q96WT3|FET3_CANGA	3.67e-259	7	630	7	629	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|E9R598|FETC_ASPFU	2.51e-206	12	584	15	576	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000239	0.999714	CS pos: 18-19. Pr: 0.9718

TMHMM  Annotations     

Start	End
558	580