CAZyme Information: FGRAMPH1_01T05159-p1

Basic Information

• Species: Fusarium graminearum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium graminearum
• CAZyme ID: FGRAMPH1_01T05159-p1
• CAZy Family: AA7
• CAZyme Description: cell surface ferroxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
570	HG970332|CGC8	63741.76	4.6028

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FgraminearumPH-1	14145	229533	2	14143

• Gene Location: location=HG970332:7010846-7012781(-)

Full Sequence      

MRFGWAVLFTPAVLAATVSYDFTIEWVRADPDGEFERPTIGINGKWPIPRIEANVGDTVL
VNARNNLGNQSTSLHFHGLFMNGSNHMDGPSQVTQCAIRPGESFLYNFTITQPGTYWYHS
HTESQYPDGLRGPLIIHDPESPFKDQYDEEIIMTISDWYHDQMQTLIPEFMRKGNPTGAE
PVPQAALMNETQDLQVDVQPGKTYLLRLANIGAFAGHFFWIEGHNLTIVEVDGAYTKPAP
ANMVYLSAGQRCSVLITTKENTLDNFPIVSSMDTDLFDVLPEDLNWNVTGWLVYDQQKDL
PEPLIVHEFDPYDDMDLVPYDDMARLPEPSKHIELDVVMDNLRDGANYAFFNNITYRAPK
VPTLYTALTSGKEATNPQIYGTYTHSFVLEKDEIVQIVVNNRDDGRHPFHLHGHHFQVLH
RSEDDVGDFTGSEEFAETPMRRDTVVVRGNGNAVLRFKADNPGLIATFVEDPLALQASLK
LPQNHLDACKAGGVPTVGNAAGNKNLLDLTGENVPPPRLPEGFTLKGIVAFTFSTLMGIF
GIYTVASYGMKKEKKTPERAPLLAEELPEQ

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	36	372	2e-151	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259945	CuRO_2_Fet3p_like	1.32e-76	149	295	1	147	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.
225043	SufI	3.43e-73	11	463	29	426	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].
259920	CuRO_1_Fet3p	1.49e-69	18	137	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.
259966	CuRO_3_Fet3p	3.85e-69	333	472	4	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.
274555	ascorbase	3.80e-64	17	466	1	504	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
SCB64374.1|AA1_2	0.0	1	570	1	570
CZS77652.1|AA1_2	0.0	1	570	1	585
QPC67749.1|AA1_2	0.0	1	570	1	585
QPC76630.1|AA1_2	0.0	1	570	1	586
CEI66016.1|AA1_2	0.0	1	570	32	617

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	2.58e-165	17	522	2	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	3.85e-64	21	496	7	485	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]
1V10_A	4.49e-61	10	463	16	467	Chain A, Laccase [Rigidoporus microporus]
5LDU_A	5.46e-60	21	463	7	447	Recombinant high-redox potential laccase from Basidiomycete Trametes hirsuta [Trametes hirsuta]
3FPX_A	1.47e-59	21	463	7	447	Native fungus laccase from Trametes hirsuta [Trametes hirsuta],3V9C_A Type-2 Cu-depleted fungus laccase from Trametes hirsuta at low dose of ionization radiation [Trametes hirsuta]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|K7NCS2|FETC_EPIFE	2.00e-263	15	565	20	593	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	1.18e-257	15	549	22	576	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
sp|E9R598|FETC_ASPFU	2.37e-235	15	550	20	573	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|P38993|FET3_YEAST	8.63e-178	15	559	21	592	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|Q6CII3|FET3_KLULA	4.17e-177	15	558	25	596	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000451	0.999552	CS pos: 15-16. Pr: 0.9797

TMHMM  Annotations     

Start	End
527	549