CAZyme Information: CAWG_04440-T-p1

Basic Information

• Species: Candida albicans
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida albicans
• CAZyme ID: CAWG_04440-T-p1
• CAZy Family: GT34
• CAZyme Description: Ortholog(s) have role in cellular response to iron ion, cellular response to iron ion starvation and fungal-type vacuole membrane localization

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
620	Supercontig_1.6_C_albicans_WO-1|CGC2	70882.86	4.4189

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CalbicansWO1	6160	294748	0	6160

• Gene Location: location=Supercontig_1.6_C_albicans_WO-1:73751-75613(-)

Full Sequence      

MIFNQFILWLISIPLILASGTIHRFDWNVSYVMANPDGIHPRRMIGINNQWPNPTIRIKK
NDQVIINLTNELPDKNVSLHFHGLFQRGYNDQDGPAFVTQCPISPGVTFTYDFNVTDQSG
TYWYHSHMGSQYGDGLRGLFIIEYDNDDEYNKEFPYDYDEDVTLSVGDHYHLESPEIVKN
FMTRFNPTGAEPIPQNGLFNETKNVTWQVNPDTTYLLRIVNMGLFTSHYVYIEDHTFTIV
EVDGVVVEPYETDSLYVAVAQRYVVLMKTKKSTDKNFRFVNVLDQDMLDFLPSDLQIVST
NWIVYDKSLELPPALPFNQFHKTIKSLVGFDDFDLRPLRKVNLLDEPDYTIQVNLTMEVL
GDGVTYAMFNGKTFRPPKVPSLYTVLSTHGNTNLTTNELIYGTNTNSFVLQGDEVVEIIL
NNMDPGKHPFHLHGHNFQVISRFDTDDEDNQLVFDPTNETYTNYPEFPMVRDTVEVGPNG
FIVLRFKADNPGVWFFHCHVDWHLEQGLAILLVEDPLELLSSNTTIPQNHIDACNAIGMP
IKGNAAGNDIDLLDLHGENIQPNPLPAGFTNKGYLAITCCTLIAIYGLWSIYNYGMEDIS
KDNAEDVIEKLYKILDDYDK

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	42	389	4.8e-145	0.9881305637982196

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	2.65e-82	22	516	35	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].
274555	ascorbase	1.99e-75	22	514	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.
259966	CuRO_3_Fet3p	2.36e-74	348	516	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	6.50e-73	160	307	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.
259920	CuRO_1_Fet3p	2.94e-71	23	142	1	120	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
AOW29490.1|AA1_2	0.0	1	620	1	620
CAX41429.1|AA1_2	0.0	1	619	1	620
CCG24206.1|AA1_2	4.02e-312	17	619	16	611
CCE85919.1|AA1_2	1.24e-272	25	618	23	609
ABN68144.2|AA1_2	1.70e-272	15	615	14	610

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	6.85e-189	23	568	3	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]
2QT6_A	2.31e-70	26	534	7	487	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
1V10_A	5.62e-70	26	527	27	502	Chain A, Laccase [Rigidoporus microporus]
4JHU_A	1.17e-69	26	534	7	485	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]
5LDU_A	1.75e-69	26	534	7	488	Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P78591|FET3_CANAX	2.00e-230	4	610	6	591	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|P38993|FET3_YEAST	1.81e-198	17	612	18	598	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|Q6CII3|FET3_KLULA	3.51e-197	18	605	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|Q96WT3|FET3_CANGA	9.18e-196	13	610	3	607	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	8.52e-188	1	615	1	612	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
0.000561	0.999411	CS pos: 20-21. Pr: 0.7468

TMHMM  Annotations     

Start	End
573	595