CAZyme Information: XP_001910797.1

Basic Information

• Species: Podospora anserina
• Lineage: Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora anserina
• CAZyme ID: XP_001910797.1
• CAZy Family: GH71
• CAZyme Description: Podospora anserina S mat+ genomic DNA chromosome 2, supercontig 2 [Source:UniProtKB/TrEMBL;Acc:B2B497]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
549		61005.77	6.6264

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PanserinaSmat	10888	515849	370	10518

• Gene Location: location=CU640366:219898-221730(-)

Full Sequence      

MKSSGVLSLAALSFATAVKAATVTYDWTATWVWAAPDGVGRPVVGINNAWPCPQIDATVG
DTVIINFTNNLGNQTSGLHFHGINQVQTPEMDGPSGVTQCPVPPGSTLQYKFVVDVGGTF
WCKFGSTAMLNLTSDRYHNESLTMVRNMLQPSNTRFAPPIPDGMIINEGAGLNVNFTKGR
KYRFRMISFAALASAMIHFDSHDINIIMNDADYLQKEVKYQLRIATAQRYDFIIECIDRD
NDNYPFLISLDINRDWTNPDLGPLQWPHNYTGYLTMDYNKPNTKKDVVHKWKPADDSHFK
PYDNEAILGGNDTNYDTLIKMDFAFCTDANGYPRACFNNLTYIDQKVPALYSAATTGDDN
SNPIVYGQINPFIVNYGDVVQIVVNNQDAATHPFHLHGHHFQVLDRPKTGTGDWSGRDTN
YNQKPPRRDTVTVMAHSHAVLRFKATNPGTWLFHCHIEWHVEMGLTATIIEAPDRLRNLT
FPQDHLDACNKMGIPVSGNAAGNTQDYLDTTGMVTVPPTIYNGAMYAGSSSKKRGLMGKL
ASGMGSFFF

Enzyme Prediction     

EC	1.10.3.2:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	39	465	1.4e-65	0.9776536312849162

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
259966	CuRO_3_Fet3p	8.49e-76	314	473	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.
259945	CuRO_2_Fet3p_like	2.13e-54	134	278	8	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.
225043	SufI	2.61e-48	2	473	6	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	3.19e-48	6	476	8	551	L-ascorbate oxidase
274555	ascorbase	4.39e-47	25	479	4	531	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
CDP25016.1|AA1_2	0.0	1	549	1	575
VBB75073.1|AA1_2	0.0	1	549	1	575
AEO62279.1|AA1_2	7.35e-255	7	530	11	548
EAA28691.3|AA1_2	3.87e-236	7	523	6	544
UQC85338.1|AA1_2	5.76e-229	8	526	4	543

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZPU_A	1.67e-89	22	512	2	523	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]
5LM8_A	2.15e-43	34	487	35	519	Crystal structure of a laccase-like multicopper oxidase McoG from from Aspergillus niger [Aspergillus niger]
5LWW_A	2.18e-43	34	487	36	520	Crystal structure of a laccase-like multicopper oxidase McoG from Aspergillus niger bound to zinc [Aspergillus niger]
5LWX_A	4.32e-43	34	487	63	547	Crystal structure of the H253D mutant of McoG from Aspergillus niger [Aspergillus niger]
4JHU_A	6.98e-40	35	489	16	485	T2-depleted laccase from Coriolopsis caperata soaked with CuCl [Coriolopsis caperata],4JHV_A T2-depleted laccase from Coriolopsis caperata [Coriolopsis caperata]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|W3X7K0|PFMAD_PESFW	9.46e-185	8	534	8	556	Multicopper oxidase PfmaD OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=PfmaD PE=2 SV=1
sp|K7NCS2|FETC_EPIFE	1.15e-128	20	517	20	542	Iron transport multicopper oxidase fetC OS=Epichloe festucae (strain E2368) OX=696363 GN=fetC PE=2 SV=1
sp|I1RMG9|FET3_GIBZE	9.33e-118	19	518	21	548	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	1.37e-115	19	517	19	539	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|Q4WZB4|ABR1_ASPFU	9.69e-108	26	506	24	535	Multicopper oxidase abr1 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=abr1 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000233	0.999752	CS pos: 20-21. Pr: 0.9764

TMHMM  Annotations     

There is no transmembrane helices in XP_001910797.1.