CAZyme Information: C6_00440C_A-T-p1

Basic Information

• Species: Candida albicans
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida albicans
• CAZyme ID: C6_00440C_A-T-p1
• CAZy Family: GT32
• CAZyme Description: Ferroxidase [Source:UniProtKB/TrEMBL;Acc:A0A1D8PPC9]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
625	Ca22chr6A_C_albicans_SC5314|CGC6	70898.01	4.2561

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CalbicansSC5314	6468	237561	256	6212

• Gene Location: location=Ca22chr6A_C_albicans_SC5314:76654-78531(-)

Full Sequence      

MRATLTSLLVSITFLVSLVAAETHTWYFKTGWVNANPDGVYERPMIGFNDTWPLPTLRVK
KGDRVQLYLINGFDNLNTTLHFHGLFQNGTNQMDGPEMVTQCPIPPGETYLYNFTVDQVG
TYWYHSHTAGQYGDGMRGVFVIDDDDFPYDYDEDVVLTVGDHYHKYSSDIIPSFLSRFNP
TGAEPIPQNFLFNETRNLTWKVEPGKTYLVRIVNVGGFVSQYLWMEDHEFTVVEVDGIYV
EKNTTDMLYITTAQRYSVLINTKNSTDKNYAFMQRVDTDMLDVIPSDLQLNGTNYIVYNE
DASLPEAYDVDSLDNYLDDFYLKPLSKEKLLDDADYTITVDVQMDNLGNGVNYAFFNNIT
YTTPKVPTLLTVLSAGDAATNELVYGTNTNSFVLQGGDVVDIVLNNLDTGKHPFHLHGHA
FQLIERHKEIPEGEDPVTYNATDHADWPEYPMVRDTVYVRPQSYIVMRFKADNPGVWFFH
CHIEWHLEQGLAFQLIEDPQGIQKNEKITDNHKQICEKVGVPWEGNAAANSKDYLNLVGE
NVQVKRLPTGFTAKGIVALVFSCISAFLGLAAISYYGMNDIENMEKRVARDLDVYFDDDD
DDEEEEEQSITEQAATGSSSSPSNK

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	42	377	1e-159	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	3.06e-96	20	499	32	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	1.54e-80	335	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.
259945	CuRO_2_Fet3p_like	5.52e-78	155	300	3	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	1.24e-67	24	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.
274555	ascorbase	1.09e-66	37	510	15	533	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOW29993.1|AA1_2	0.0	1	625	1	625
CAX40993.1|AA1_2	0.0	1	597	1	597
CAX40994.1|AA1_2	0.0	1	594	1	595
CAX40995.1|AA1_2	0.0	1	594	1	597
AOW29995.1|AA1_2	0.0	1	593	1	596

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	2.35e-255	22	550	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	1.19e-65	34	516	14	491	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]
5EHF_A	2.06e-65	33	526	11	496	Laccase from Antrodiella faginea [Antrodiella faginea]
1V10_A	4.99e-65	34	518	34	510	Chain A, Laccase [Rigidoporus microporus]
1GYC_A	2.19e-64	36	516	16	488	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	1	593	1	594	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|Q6CII3|FET3_KLULA	1.14e-281	5	592	9	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|Q96WT3|FET3_CANGA	7.31e-274	13	592	9	597	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|P38993|FET3_YEAST	6.18e-273	1	594	1	599	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|E9R598|FETC_ASPFU	1.11e-220	14	581	11	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
0.000293	0.999693	CS pos: 21-22. Pr: 0.9792

TMHMM  Annotations     

Start	End
555	577