CAZyme Information: Z517_06772-t43_1-p1

Basic Information

• Species: Fonsecaea pedrosoi
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Fonsecaea; Fonsecaea pedrosoi
• CAZyme ID: Z517_06772-t43_1-p1
• CAZy Family: GH31
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
533	KN846972|CGC7	56969.43	7.3843

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FpedrosoiCBS271-37	12573	1442368	46	12527

• Gene Location: location=KN846972:2691784-2693661(+)

Full Sequence      

MVRTFFRTARLAVVLSACLLVSAQADELDLSAPIEVLDSSPPIEELEISATTDSVSTQSV
SFNGCSALSSAGLRSLLLYPSDPAYASREASYWSPIAALGPQCIIQPRSTADVSKVVKAL
ARAKAKFAVRSGGHVLWAGGSDIKDGVTIDLGLMTAVTYNSQTKIVSIQPGPRWGDVYNT
LAPLGVTVTGGRDAGVGIGGFLTGGGLSFLSGRNGLACDQVVRFEVVLADGRIVHADYTS
NRDLWKALKGGWANYGIVTRFDVTSTPLTTAWGGFNLHDKSVGPQVTTALVNFINNLRQT
PDNAHLALAAYNSFIPGETSIGTFAINTLGVENATALREILQVPAIARDLDFLTLGEIGE
KFKDPSDDRVIWHTLTFNNDVNIANKALALHDELVARLKSTLGADKFNSQCVLQPLPSLF
AEIGARQGGNVLGLDSVNRNSILWVGSVGFQNAAYQQAAHDAVSAYARNLESYAQSRNGN
VAFRYINYADKDQNPLKSYGSTNVNFIKRVATKYDPTGVFQKQVPGSFKVSAI

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	90	522	1.1e-56	0.982532751091703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	3.29e-22	80	520	15	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	3.99e-20	101	237	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.
178402	PLN02805	6.58e-07	101	259	134	298	D-lactate dehydrogenase [cytochrome]
215242	PLN02441	1.72e-06	59	260	20	233	cytokinin dehydrogenase
273751	FAD_lactone_ox	1.69e-05	93	303	7	202	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
BAI44126.1|AA7|CBM18	9.48e-20	101	520	275	710
QBZ61916.1|AA7|CBM18	1.26e-19	101	520	275	710
CAI94231.1|AA7|1.1.3.-	2.21e-19	101	267	59	228
UJO16207.1|AA7	1.60e-18	101	270	128	299
UJO23499.1|AA7	2.78e-18	79	267	41	230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	1.09e-20	70	308	15	248	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]
6FYF_A	1.96e-20	70	308	15	248	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	1.96e-20	70	308	15	248	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]
6FYE_A	2.62e-20	70	308	15	248	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
3RJ8_A	2.77e-20	101	267	37	206	Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A0U5GQ05|DRTC_ASPCI	8.05e-89	65	533	45	516	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|C8VPE5|SDCF_EMENI	7.32e-84	65	530	8	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|M2T7Z1|TPCD_COCH5	8.73e-64	79	531	56	518	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|G3Y424|YANF_ASPNA	4.05e-50	81	531	134	577	FAD-dependent monooxygenase yanF OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=yanF PE=1 SV=1
sp|A0A2P1DP98|MACF_PENTR	1.21e-45	93	522	84	507	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
0.000417	0.999564	CS pos: 25-26. Pr: 0.9637

TMHMM  Annotations     

There is no transmembrane helices in Z517_06772-t43_1-p1.