CAZyme Information: KNX49983.1

Basic Information

• Species: Cryptococcus gattii VGII
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus gattii VGII
• CAZyme ID: KNX49983.1
• CAZy Family: GT69
• CAZyme Description: ferroxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
639		70844.74	4.6184

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CgattiiVGIIR265	6705	294750	281	6424

• Gene Location: location=CP025759:1879099-1881635(-)

Full Sequence      

MPTLSFLFLASATAASVATAAVHDLYWNITYATANPDQLHNKTQAIGVNGTWPPPPIVVN
QGDTLTVHAFNGLGSVGTTLHSHGNYFNGSNYYDGAAAVTQCPIPPGETLVYEIPVNDQW
GTYWIHGHYNGQYVDGLRAPLIIMPNKTTERTDITWDEDFTIIMGDWYHDTSPYLVSSYF
LNWVNPTGAEPIPDSVAFYVMNTTSGEYMSRNIAQGVDVSADVNNNAAIPFEPGKKYRIR
FINMSALSMLHIYMGGHTFDIIEVDAVDIEPYQSTNLTVSVAQRYSILVEALNTTDANYA
IMFYQDTDMYDTVPDALAVNNSVTLQYDASLGPADMFNITDDTWPMLDDTRFVPLQAKRS
AEADVSYELGAYFDTFDDGTNRAAFNNITYVMPTTPSLFTQISMGTDAWDTRIYGQQTHA
LMMPHLEMIELVIVNWDTGYHPFHLHGHEFQIMAKSFDVTSNDTSINPPVLEKQSNPARR
DTIMVPPGGSVHIRFRADNPGAWIFHCHIDWHMDSGLAVIMITDPSYSQLSLKIPQTMKD
HCEYWGYSATGNVVGLNSTTDFKGEAIGPLPLVMDWTPKAKGALAGCIIAALAGFASVVW
YGAEHLDEKEIEAEIRRKAEIKAASGGKFGMIKKMAKRE

Enzyme Prediction     

No EC number prediction in KNX49983.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	44	406	2.2e-129	0.9881305637982196

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259966	CuRO_3_Fet3p	3.97e-90	364	525	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.
259920	CuRO_1_Fet3p	2.77e-69	23	144	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.
274555	ascorbase	4.31e-67	27	520	6	520	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.
225043	SufI	6.60e-62	47	525	56	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].
177843	PLN02191	2.45e-60	26	522	27	545	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
KNX49983.1|AA1_2	0.0	1	639	1	639
AUB23306.1|AA1_2	0.0	1	639	1	639
AFR93734.1|AA1_2	0.0	1	639	1	639
UOH79935.1|AA1_2	0.0	1	639	1	638
KGB79104.1|AA1_2	6.37e-243	15	624	15	625

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	7.50e-101	23	567	3	526	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	1.17e-63	29	542	10	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]
3SQR_A	1.70e-63	26	545	70	564	Crystal structure of laccase from Botrytis aclada at 1.67 A resolution [Botrytis aclada],4X4K_A Structure of laccase from Botrytis aclada with full copper content [Botrytis aclada]
3V9E_A	3.27e-63	26	545	70	564	Structure of the L499M mutant of the laccase from B.aclada [Botrytis aclada]
5NQ7_A	2.33e-61	4	542	8	507	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4PIF8|FER1_USTMA	2.36e-186	1	602	10	614	Iron multicopper oxidase fer1 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=fer1 PE=2 SV=1
sp|E9R598|FETC_ASPFU	8.49e-134	19	602	19	572	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|Q09920|FIO1_SCHPO	1.63e-122	27	610	29	591	Iron transport multicopper oxidase fio1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=fio1 PE=3 SV=1
sp|P78591|FET3_CANAX	1.35e-121	15	609	16	588	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|K7NCS2|FETC_EPIFE	9.42e-118	14	602	12	575	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000284	0.999677	CS pos: 20-21. Pr: 0.9640

TMHMM  Annotations     

There is no transmembrane helices in KNX49983.1.