CAZyme Information: AGR57_5094T0-p1

Basic Information

• Species: Phanerochaete chrysosporium
• Lineage: Basidiomycota; Agaricomycetes; ; Phanerochaetaceae; Phanerochaete; Phanerochaete chrysosporium
• CAZyme ID: AGR57_5094T0-p1
• CAZy Family: GH35
• CAZyme Description: FAD-binding domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
483		50986.27	4.8692

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PchrysosporiumRP-78	13602	273507	0	13602

• Gene Location: location=PchrRP-78_SC004:2198453-2200370(+)

Full Sequence      

MRRSTVVALLAGSALAKAGASASDTCHSIAKAVSKASDVYWPGSLSYTNGIKHWATSSTA
LAACSVEPGSAGDIGKILQILGSTKTPFAVKGGGHSTNAGFSSTTGVHIAMSRFKNVTYN
SAAQTVDYGTGITWDAVYEALEPFGVNVVGGRVSGVGVAGFSLGGGYSWLTNQYGLTVDN
IVGFQIVLPNGQVTDVTRESDSDLFFSVLGGYNNFGIVTRFTAKAYPQGQVWGGNKFVLG
LGDNWEKLNEATAKFQAEVTDPKAQVLPTYNVAEGTAVASVLMFYDGPTPPEGIFDDFLA
IPALSSDIATRSFLSLVQSTPSTATTRAVFDTVSLTTISPALLEAVVNETQFWSARLALR
SANFLSYDVEPFLTSLFKHGAEAATAYPPTRERGLLPLNIYYAWDLAEFDEAMQAAAAQS
AAHLRAVALAAGEDIADVPVYGNYAGPNTPVEQIFGDSLPRMRETKQRVDPNDVMGLAGG
WKV

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	62	256	7.5e-45	0.4170305676855895

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	1.92e-16	62	197	1	139	FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
223354	GlcD	2.19e-16	55	475	25	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
215242	PLN02441	1.00e-06	59	220	62	233	cytokinin dehydrogenase
178402	PLN02805	1.14e-05	66	231	138	312	D-lactate dehydrogenase [cytochrome]
273751	FAD_lactone_ox	0.007	52	228	5	181	sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UJO18775.1|AA7	9.77e-17	29	224	39	237
UJO23499.1|AA7	1.18e-14	61	474	62	476
QRC92907.1|AA7	2.11e-14	39	226	40	230
QGA17347.1|AA7	1.95e-13	36	262	21	250
CAE7214923.1|AA7	4.84e-13	39	230	40	234

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	1.16e-17	38	231	21	214	The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
6EO4_A	1.66e-17	91	226	77	216	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
6EO5_A	1.66e-17	91	226	77	216	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6FYF_A	2.08e-17	38	231	21	214	The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_B The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_C The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_D The crystal structure of EncM V135M mutant [Streptomyces maritimus]
6FYG_A	2.08e-17	38	231	21	214	The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4B1P2|A2372_ARTBC	4.69e-53	31	317	31	319	Uncharacterized FAD-linked oxidoreductase ARB_02372 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02372 PE=1 SV=1
sp|A0A0U5GQ05|DRTC_ASPCI	4.92e-46	39	483	57	513	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|A0A2V5HCN7|PYVE_ASPV1	1.60e-39	39	474	15	442	FAD-linked oxidoreductase pyvE OS=Aspergillus violaceofuscus (strain CBS 115571) OX=1450538 GN=pyvE PE=3 SV=1
sp|C8VPE5|SDCF_EMENI	5.74e-37	39	483	20	476	FAD-dependent monooxygenase sdcF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=sdcF PE=1 SV=1
sp|A0A2P1DP98|MACF_PENTR	4.80e-36	54	306	84	333	FAD-dependent monooxygenase macF OS=Penicillium terrestre OX=374132 GN=macF PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000347	0.999599	CS pos: 18-19. Pr: 0.9778

TMHMM  Annotations     

There is no transmembrane helices in AGR57_5094T0-p1.