CAZyme Information: EEQ91777.2

Basic Information

• Species: Blastomyces dermatitidis
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Blastomyces; Blastomyces dermatitidis
• CAZyme ID: EEQ91777.2
• CAZy Family: GH47
• CAZyme Description: FAD binding domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
534		58965.81	5.8275

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BdermatitidisER-3	10081	559297	326	9755

• Gene Location: location=EQ999979:2701372-2703111(-)

Full Sequence      

MRSSCYSALVSILLGWHSLAFKSPDIHPSSPPVSQDDPLEKVPSFPKFNETNAIPRRCEL
ACSYLSKTYADTVAFPGSDKYSRFQTSFWSQQQSKVSPMCIFRPENVKQVSFAMFVNTEI
NCTFAVRSGGHATFPGASNIQDGMTFDMQAINEITISPDGKTAVLGTGNTWYDVYKTLEV
NNMTAVGASAADVGVGGHILGGGISLLSNMYGWGCNNVINYEIIGAHGGILNVDAERPEM
FFALCGGGNNFGIVTRFTVKIYPQSLMWQGVRGFSIHQKRVVLDAYVSLGRNINKDPRSS
NHLTAFTVTSDAERISVYLENADGIPYPAIFDEVKAIPTIFATSKVQYMSEITKTLENEA
PSGLRNTHWTYTFKLDAWLVGFVTDTFLAAIQPVRNISGIIADCRFQTLTESMLLHMKGK
VFGLSSEGGPYTLLLLSATWSDEADDKMIYRAFSDMLQAIKEEAKQSGLHVDYLFMNYAS
QFQDVISSYGAENVQRLRVASYNDDPEGFLERLQPGYFKLNGSAPAKMREDGLN

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	89	286	7.1e-45	0.4344978165938865

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	3.54e-10	98	234	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	1.28e-09	98	263	32	205	FAD/FMN-containing dehydrogenase [Energy production and conversion].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UNI23960.1|AA7	8.16e-18	73	263	24	216
UJO18775.1|AA7	1.71e-15	96	260	71	237
QUC19098.1|AA7	4.50e-15	73	295	24	249
UPK90596.1|AA7	5.32e-14	96	514	18	439
QGA17347.1|AA7	1.39e-13	49	260	3	213

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EO4_A	1.63e-19	74	265	26	219	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
6EO5_A	1.63e-19	74	265	26	219	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6FYD_A	8.51e-19	100	525	51	460	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]
6FYB_A	2.02e-18	100	525	51	460	The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus]
6FYG_A	2.02e-18	100	525	51	460	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|M2T7Z1|TPCD_COCH5	2.05e-79	58	521	30	518	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|A0A023I4D6|PRX3_PENRO	1.41e-65	53	523	23	510	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
sp|W6Q5R7|PRX3_PENRF	1.41e-65	53	523	23	510	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1
sp|A0A0U5GQ05|DRTC_ASPCI	1.35e-64	55	530	33	523	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|B6H064|PRX3_PENRW	3.06e-62	61	523	31	510	FAD-dependent monooxygenase prx3 OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=prx3 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000364	0.999594	CS pos: 20-21. Pr: 0.9689

TMHMM  Annotations     

There is no transmembrane helices in EEQ91777.2.