CAZyme Information: SPAC1F7.08.1-p1

Basic Information

• Species: Schizosaccharomyces pombe
• Lineage: Ascomycota; Schizosaccharomycetes; ; Schizosaccharomycetaceae; Schizosaccharomyces; Schizosaccharomyces pombe
• CAZyme ID: SPAC1F7.08.1-p1
• CAZy Family: GH13|GH13
• CAZyme Description: plasma membrane iron transport multicopper oxidase Fio1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
622	Spom972h_chrI|CGC1	69907.66	4.0122

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Spombe972h	6995	284812	1857	5138

• Gene Location: location=Spom972h_chrI:4235639-4237507(+)

Full Sequence      

MNKFFSFPILGLLLTCVRFVVAKERLFEWNVTDVYDVDPDGSGNSRWVIGVNNKWPIDPL
VVDYGDQVIIKMTNSLANNRTTSLHSHGLFQKFTPYMDGVPQSTQCEIPPGATFYYNYTA
LQNGTYWVHSHDMSQYPDGLRTPFIINALEEPYDYDEEYIISMTDWYYTPFNILVPDEFK
TWKNPTGAEPVPDTGLFNDTANATFAMEPGKTYRLRFINIGAFNNYDVMIEDHNMTIIEV
DGEYTEPQEVSSIHLTVAQRYSVLVTAKNSTDRNYAITAYMDESLFDTIPDNYNPNVTAW
LSYNSDASYDLGPDIDEIDSYDDAELNPLYSWDVTESNHSINIWFDFFTLGDGANYAEIN
DSSYVFPKVPSIMIANSTNVDGYNLEPVTYGPYTNAYIFEYGDVVDVIIDNHDTGKHPFH
LHGHTFQVLERGEENAGLYSDQESHTYYDNPMRRDTVEIEPGSFIVIRFIADNPGAWVIH
CHIEWHMESGLLATFIEAPEMIPSISSPDFVKEQCMLDGVPTIGNGAGNYKNISDLSGAP
SPPGEMPAGWTSKAIGTMAACVISACIGMGSIIFYGASIHPVPTEELDENDDLQEAALEN
AAMFLDTDKAVEKVVEGKDEIK

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	46	379	3.5e-131	0.9881305637982196

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	9.93e-104	5	500	19	451	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	1.41e-85	337	499	2	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	2.27e-73	157	305	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	1.99e-65	25	507	2	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.
215324	PLN02604	1.00e-60	7	507	5	556	oxidoreductase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
NP_594494.1|AA1_2	0.0	1	622	1	622
BAE61606.1|AA1_2	8.55e-178	20	589	28	595
UDD60384.1|AA1_2	3.49e-177	20	589	18	585
QMW43510.1|AA1_2	3.36e-176	20	575	18	571
QMW31452.1|AA1_2	3.36e-176	20	575	18	571

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	3.55e-128	23	549	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]
1V10_A	3.47e-62	36	503	34	495	Chain A, Laccase [Rigidoporus microporus]
1HFU_A	3.25e-60	36	497	15	468	Chain A, LACCASE 1 [Coprinopsis cinerea]
1A65_A	3.32e-60	36	497	15	468	Chain A, Laccase [Coprinopsis cinerea]
3KW7_A	2.29e-59	36	497	14	472	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q09920|FIO1_SCHPO	0.0	1	622	1	622	Iron transport multicopper oxidase fio1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=fio1 PE=3 SV=1
sp|E9R598|FETC_ASPFU	1.04e-173	22	590	20	592	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	7.83e-159	11	578	9	577	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	3.62e-148	22	578	22	578	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|Q4PIF8|FER1_USTMA	1.42e-143	8	576	11	614	Iron multicopper oxidase fer1 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=fer1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000511	0.999462	CS pos: 22-23. Pr: 0.9778

TMHMM  Annotations     

There is no transmembrane helices in SPAC1F7.08.1-p1.