CAZyme Information: C6_00480C_A-T-p1

Basic Information

• Species: Candida albicans
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida albicans
• CAZyme ID: C6_00480C_A-T-p1
• CAZy Family: GT34
• CAZyme Description: Fet31p [Source:UniProtKB/TrEMBL;Acc:A0A1D8PPE2]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
619	Ca22chr6A_C_albicans_SC5314|CGC8	70571.49	4.3773

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_SC5314:87450-89309(-)

Full Sequence      

MRSLSIFSLVFLFFSTLITAKTHTWYYKTGWVNANPDGGFERPMIGFNDSWPLPTLRVKK
GDTVNLYLINGFDDRNTSLHFHGLFQHGTNQMDGPEMVTQCPIPPGETFLYNFTVDDQVG
SYWYHSHTSGQYGDGMRGVFIIEDDDFPYDYDEEVILTLGEHYHDFSDDLHKNFMSRYNP
TGAEPIPSNILFNETRNNTWKVEPGKTYFVRIINIGRFVSQYVWMEDHEFTIVEVDGIYV
EKNTTDLIYITVAQRYGVLITTKNSTDKNYAFMNRVDIDMLDVIPDELELNGTNYIEYNS
KADKPEPYLLDSIDDYFDDFYLKPLSKEKLLDDADYTITVDVQMDNLGNGVNYAFFNNIT
YTTPRVPTLLSVLSAGDDASNELVYGTNTNSFVLQSGDVVDIVLNNLDTGKHPFHLHGHV
FQLIERHEEIPETEDPVGYNASDHADWPEYPMLRDTVYVRPQSYIVMRFKADNPGVWLFH
CHIEWHLDQGLAIQLIEDPQGIQKNASQHITDNHKQICEKVGVSWEGNAAANSKDYLNLK
GENVQHKRLPTGFTARGIVALVFSCIAGVLGLATIAYYGMNDIADVEERVARDLDVDFDE
EDNEIVNEGSSSSGSNSKH

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	41	377	1.9e-158	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	3.30e-98	20	499	33	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	7.79e-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	1.91e-74	153	300	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	1.29e-68	36	504	15	527	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.
259920	CuRO_1_Fet3p	1.64e-68	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
AOW29996.1|AA1_2	0.0	1	619	1	619
CAX40996.1|AA1_2	0.0	1	618	1	618
CAX40995.1|AA1_2	0.0	5	599	6	600
AOW29995.1|AA1_2	0.0	13	595	14	596
CAX40993.1|AA1_2	0.0	13	616	14	620

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	2.98e-247	21	552	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]
2QT6_A	2.59e-65	33	505	12	477	Chain A, Laccase [Lentinus tigrinus],2QT6_B Chain B, Laccase [Lentinus tigrinus]
5EHF_A	3.53e-65	32	498	11	468	Laccase from Antrodiella faginea [Antrodiella faginea]
3KW7_A	1.52e-63	33	498	14	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]
5Z1X_A	2.53e-62	36	518	17	484	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P78591|FET3_CANAX	0.0	4	595	5	594	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|Q6CII3|FET3_KLULA	3.57e-286	15	599	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|Q96WT3|FET3_CANGA	1.02e-274	13	594	10	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	1.01e-267	8	597	7	600	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|E9R598|FETC_ASPFU	2.93e-219	7	583	5	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
0.000259	0.999715	CS pos: 20-21. Pr: 0.9805

TMHMM  Annotations     

Start	End
5	27
557	579