CAZyme Information: MRET_0002-t46_1-p1

Basic Information

• Species: Malassezia restricta
• Lineage: Basidiomycota; Malasseziomycetes; ; Malasseziaceae; Malassezia; Malassezia restricta
• CAZyme ID: MRET_0002-t46_1-p1
• CAZy Family: AA1
• CAZyme Description: iron transport multicopper oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
559	CP030251|CGC2	62376.65	8.1244

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MrestrictaKCTC27527	4544	N/A	138	4406

• Gene Location: location=CP030251:2502-4181(-)

Full Sequence      

MKFHLAISAAFAAGAYAADVGKHWKIGWIDNVNPDGKFPRRAIGINGKFPHDPVSINSND
FLHINVSNAFGDGRPTTLHAHGLYYQNVNYFDGAANVAQCPIPDGQSFNYEILNSPRAGK
TESQWGTYWLHGHYKGQYTDGLRTPFIIHNANGEVYDYDDDYTVALTDWYHEEHGYLKHH
KFLKPDPIYPTPKEGLMYFAHTKANQTAKNLPGYNENATLPFEPGKTYRLRLINMSAASR
FDFWIEGHDMDIIEADGTDVKRFATDVVQVGIGQRYSVLVKARNSAENDWRIHADMEKDM
YGGGFKHQDGDHLRLNLTSKVSYGKKNAKLGKGRKTISTFKLFDDLLLEPVHKESAETKP
DMAVTLMVGMNSTEDGIPIGTFNGTQFKAPLTPPILTMKTENDTAIMDPKIYGPNSNAVV
APYNSTVELKLVSAGGAHPFHLHGTKFQLVERMKNTSLPCTKQCSRENPLRRDTVILPAG
GSVTMRFRADNPGAWMMHCHMDWHLAAGLAMMVIQAPREAKKMLDVPSYFPQQCRMQGLP
VHGNAGGVRGSTTDFGRLN

Enzyme Prediction     

No EC number prediction in MRET_0002-t46_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	40	403	1.8e-117	0.9910979228486647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259920	CuRO_1_Fet3p	1.79e-55	20	149	1	121	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.
225043	SufI	2.57e-54	44	512	56	443	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	1.86e-50	361	517	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.
215324	PLN02604	7.96e-46	38	509	41	540	oxidoreductase
259945	CuRO_2_Fet3p_like	5.33e-45	160	325	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AXA48447.1|AA1_2	0.0	1	559	1	559
AYO41723.1|AA1_2	0.0	1	559	1	559
SHO78811.1|AA1_2	1.30e-240	1	558	1	560
SHO79878.1|AA1_2	6.53e-202	12	558	16	567
SAM72511.1|AA1_2	3.59e-160	5	555	13	570

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.88e-82	23	517	6	481	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	7.95e-68	31	512	34	486	Chain A, Laccase [Rigidoporus microporus]
3T6V_A	2.39e-66	31	534	15	488	Crystal Structure of Laccase from Steccherinum ochraceum [Steccherinum ochraceum],3T6V_B Crystal Structure of Laccase from Steccherinum ochraceum [Steccherinum ochraceum],3T6V_C Crystal Structure of Laccase from Steccherinum ochraceum [Steccherinum ochraceum],3T6W_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (10% dose) [Steccherinum ochraceum],3T6W_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (10% dose) [Steccherinum ochraceum],3T6W_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (10% dose) [Steccherinum ochraceum],3T6X_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (20% dose) [Steccherinum ochraceum],3T6X_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (20% dose) [Steccherinum ochraceum],3T6X_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (20% dose) [Steccherinum ochraceum],3T6Z_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (60% dose) [Steccherinum ochraceum],3T6Z_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (60% dose) [Steccherinum ochraceum],3T6Z_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (60% dose) [Steccherinum ochraceum],3T71_A Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (90% dose) [Steccherinum ochraceum],3T71_B Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (90% dose) [Steccherinum ochraceum],3T71_C Crystal Structure of Steccherinum ochraceum Laccase obtained by multi-crystals composite data collection technique (90% dose) [Steccherinum ochraceum]
6RHH_A	6.98e-66	31	534	15	488	Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RHI_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RHO_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RHP_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Twenty first structure of the series with 4415 KGy dose (collected after refreezing). [Steccherinum murashkinskyi],6RHR_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. First structure of the series with 15 KGy dose. [Steccherinum murashkinskyi],6RHU_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Second structure of the series with 165 KGy dose. [Steccherinum murashkinskyi],6RHX_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Third structure of the series with 315 KGy dose. [Steccherinum murashkinskyi],6RI0_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Ninth structure of the series with 1215 KGy dose. [Steccherinum murashkinskyi],6RI2_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by chloride anions at sub-atomic resolution. Twentieth structure of the series with 4065 KGy dose. [Steccherinum murashkinskyi],6RI4_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. First structure of the series with 13 KGy dose. [Steccherinum murashkinskyi],6RI6_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Second structure of the series with 400 KGy dose. [Steccherinum murashkinskyi],6RI8_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Third structure of the series with 800 KGy dose. [Steccherinum murashkinskyi],6RII_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourth structure of the series with 1200 KGy dose. [Steccherinum murashkinskyi],6RIK_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Thirteenth structure of the series with 5200 KGy dose. [Steccherinum murashkinskyi],6RIL_A Single crystal serial study of the inhibition of laccases from Steccherinum murashkinskyi by fluoride anions at sub-atomic resolution. Fourteenth structure of the series with 5600 KGy dose (data was collected after refreezing). [Steccherinum murashkinskyi]
5MEW_A	7.15e-66	31	534	15	488	The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi. Second structure of the series with total exposition time 33 min. [Steccherinum murashkinskyi],6RGH_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. First structure of the series with 15 KGy dose. [Steccherinum murashkinskyi],6RGP_A Single crystal serial study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi at sub-atomic resolution. Second structure of the series with 165 KGy dose. [Steccherinum murashkinskyi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4PIF8|FER1_USTMA	4.20e-157	15	558	27	577	Iron multicopper oxidase fer1 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=fer1 PE=2 SV=1
sp|Q09920|FIO1_SCHPO	2.87e-101	24	555	29	536	Iron transport multicopper oxidase fio1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=fio1 PE=3 SV=1
sp|E9R598|FETC_ASPFU	9.20e-98	17	547	20	524	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
sp|K7NCS2|FETC_EPIFE	9.16e-95	6	559	9	539	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	5.39e-93	24	555	29	533	Iron transport multicopper oxidase FET3 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FET3 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000347	0.999637	CS pos: 17-18. Pr: 0.9728

TMHMM  Annotations     

There is no transmembrane helices in MRET_0002-t46_1-p1.