CAZyme Information: KSA04233.1

Basic Information

• Species: Debaryomyces fabryi
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Debaryomyces; Debaryomyces fabryi
• CAZyme ID: KSA04233.1
• CAZy Family: GT91
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
630	LMYN01000001|CGC1	71725.71	4.8132

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_DfabryiCBS789	6025	N/A	0	6025

• Gene Location: location=LMYN01000001:209968-211860(-)

Full Sequence      

MRLISILYCIIFALGIVAKTHTFHFNASYIIANPDGVHERRVIGINNEWPLPTIRIKKND
RVEIYLTNSLEDRNTSLHFHGLFQQESNSMDGPEMVTQCPIAPGSTFLYNFTVSEQAGTY
WYHSHSGAQYSDGLRGVFIVEDDERLPFIYDEEVTLTVSDWYHLEYPDVMSSFLSRYNPT
GAEPIPQNSLFNDTKNATWHVKPDTTYLVRIVNMGMFTSQYLYIEDHSFTIVEIDGNLVE
PVETDSLYIAVAQRISVLVHTKKSKAKNYRFVNIIDEEMLDFLPDELLIISTNWVAYNDK
ELPHPLKNGLNEFAKLTEKLKPVDDFDLRPLSKEALFPDYDYQIHLDFTMDNLGDGVNYA
LFNDITYVPPKVPTLLTVLSSGKYAGDTEIYGSNTNTHILQHNEIVEIVLNNRDAGKHPF
HLHGHNFQVISRSEAGEDEENPILYDPKNPDHTNFPDFPMVRDTVMVNPNGFIVIRFKAN
NPGVWFFHCHVDWHLEQGLAITLVEAPFEIQKSQNISSNHWDACALANISSKGNAAGKYG
DSKDIWHDLSGENLQPEPLPAGFTLKGYIAFLICSLCAVFGLYSIYKYGMEDIKNDSNEA
VVHKLYRILETHGALDESEQSALFSVNSRE

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	39	383	1.1e-152	0.9940652818991098

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225043	SufI	4.33e-99	18	508	33	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	5.87e-87	341	507	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.
274555	ascorbase	1.71e-86	23	506	4	524	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.
259945	CuRO_2_Fet3p_like	8.24e-76	152	299	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.
177843	PLN02191	3.16e-72	16	512	12	553	L-ascorbate oxidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAG88101.1|AA1_2	0.0	1	630	1	630
CCE85919.1|AA1_2	0.0	1	628	1	625
ABN68144.2|AA1_2	4.72e-313	1	616	1	617
SGZ52816.1|AA1_2	8.50e-302	16	628	16	630
SGZ51037.1|AA1_2	1.21e-301	16	628	16	630

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	6.27e-205	19	562	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]
3KW7_A	5.76e-72	34	505	17	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]
2XYB_A	1.48e-69	33	526	16	488	CRYSTAL STRUCTURE OF A FULLY FUNCTIONAL LACCASE FROM THE LIGNINOLYTIC FUNGUS PYCNOPORUS CINNABARINUS [Trametes cinnabarina]
5NQ7_A	9.31e-69	33	526	37	509	Crystal structure of laccases from Pycnoporus sanguineus, izoform I [Trametes sanguinea]
5NQ8_A	4.90e-68	33	526	37	509	Crystal structure of laccases from Pycnoporus sanguineus, izoform II [Trametes coccinea],5NQ9_A Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea],5NQ9_C Crystal structure of laccases from Pycnoporus sanguineus, izoform II, monoclinic [Trametes sanguinea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P78591|FET3_CANAX	1.76e-231	16	593	19	582	Iron transport multicopper oxidase FET3 OS=Candida albicans OX=5476 GN=FET3 PE=3 SV=1
sp|P43561|FET5_YEAST	1.63e-221	5	609	5	612	Iron transport multicopper oxidase FET5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET5 PE=1 SV=1
sp|Q6CII3|FET3_KLULA	3.36e-218	18	601	25	599	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|P38993|FET3_YEAST	1.38e-213	18	606	21	598	Iron transport multicopper oxidase FET3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=FET3 PE=1 SV=2
sp|Q96WT3|FET3_CANGA	5.58e-205	3	628	2	618	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.171348	0.828631	CS pos: 18-19. Pr: 0.7959

TMHMM  Annotations     

Start	End
567	586