CAZyme Information: KAG5418637.1

Basic Information

• Species: Candida metapsilosis
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida metapsilosis
• CAZyme ID: KAG5418637.1
• CAZy Family: GH18
• CAZyme Description: FET3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
613	JAEOAQ010000005|CGC7	69752.31	4.7514

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CmetapsilosisBP57	5743	N/A	17	5726

• Gene Location: location=JAEOAQ010000005:1000422-1002263(+)

Full Sequence      

MLSLHFILLLSCLYNIVASKTHTFDWDIGYVKANPDGMHERRMIGINNQWPNPTIRVKQH
DRVILNLYNGLPDRNASLHFHGLMQRGFNGQDGPEMVTQCPVAPGSKITYDFNVGEQTGT
YWYHSHSGSQYGDGLRGMIIIDYADKKDEPYTYDEDVSLSVNDHYHLESPQIIKQFLSRF
NPTGAEPIPQNSLFNETRNGTWHVEPDKTYLLRIVNMGLFVSQYLKIEDHKFIVVEIDGV
AVEPYEVDSLYITVGQRYAVLVKTKSQSDKNYRFINALDMEMLDVIPEDLQLVSTNYLVY
DANAPNPQHYPYYDFEKFTDSLDGFNDFDLKPLSKEKLLPEPDITIQVNFSMEVLGDGVT
YALFNDKSYVPPKVPLLYTVLSSGELSTNPQIYGSNTNTFVLQGNETVELILNNHDPGKH
AFHLHGHNFQVISRSPGTDDEDHPVEFNPHNDSMIDYPEYPMIRDTVEVNSNGYFVLRFK
ADNPGVWFFHCHVDWHLEQGLALVLVEAPEEIQAHHKHISANHVEVCKNVSVPIQGNAAA
NMDFLDLTGQNLQQAPLPEGFTTKGYIAMALCTFVAVYGIWSIYKYGIEDVSKDNTAEVI
ERLSKILDEHDGE

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	40	385	2.1e-143	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	9.27e-88	18	510	32	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].
274555	ascorbase	5.46e-83	24	512	4	528	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.
259966	CuRO_3_Fet3p	3.89e-80	343	509	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	2.80e-76	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.
215324	PLN02604	1.96e-73	6	512	8	551	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCG24206.1|AA1_2	0.0	1	612	1	612
AOW29490.1|AA1_2	8.03e-307	6	611	6	619
CAX41429.1|AA1_2	4.62e-306	1	611	1	620
ABN68144.2|AA1_2	1.10e-278	17	607	17	610
QFZ52610.1|AA1_2	4.89e-268	4	612	2	619

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	4.77e-195	20	560	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	1.07e-63	8	507	10	489	Chain A, Laccase [Rigidoporus microporus]
3KW7_A	2.64e-62	25	507	7	472	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]
5Z1X_A	4.42e-60	35	514	17	472	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]
2XYB_A	3.33e-59	25	514	7	474	CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS [Trametes cinnabarina]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P78591|FET3_CANAX	3.10e-235	6	608	8	594	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|Q6CII3|FET3_KLULA	1.77e-208	15	603	21	602	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	6.32e-205	9	603	11	597	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|Q96WT3|FET3_CANGA	9.15e-202	17	591	15	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|P43561|FET5_YEAST	8.15e-197	15	611	14	616	Iron transport multicopper oxidase FET5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000210	0.999766	CS pos: 19-20. Pr: 0.9571

TMHMM  Annotations     

Start	End
566	588