CAZyme Information: HMPREF1541_07107-t46_1-p1

Basic Information

• Species: Cyphellophora europaea
• Lineage: Ascomycota; Eurotiomycetes; ; Cyphellophoraceae; Cyphellophora; Cyphellophora europaea
• CAZyme ID: HMPREF1541_07107-t46_1-p1
• CAZy Family: GH47
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
538	KB822723|CGC2	57933.19	5.7687

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CeuropaeaCBS101466	11153	1220924	59	11094

• Gene Location: location=KB822723:69567-71230(-)

Full Sequence      

MLFRASCLVAAFAFSSWAQVTEPANFNVTEALIEEGVDITELPLADLQSRSSNAACAVAC
ASLDIIYSSNLFRDGEAAYDSFTDNYWAQQQSNVNPYCIFKAPDTKSVSVAILISRLTTC
PFAAKSGGHAAFKGASNIEGGITISLENLDSIKVSSDKKTVAIGSGNRWARVYSELAKSD
LAVIGGRVAPIGTGGLTTGGGISFFSGIYGWACDNVAAYDVILASGLTTTASPTQNPDLY
WALRGGGNNFGIVHTFHYEAIELPGNAMWGGGRVYLEDQFAGLTKAFANLVANSPKDPNA
GQWVAWLTNQGTKIASTELWYGNPNGGSAVIFNEYNNLTAISDTTGPKKLAAYATELDAS
NPYGLRETYYGLTVQADQALAEIAKDIFFEELPATANVAGANPVLLYQGITSGQIAAMRK
NGGNPLGLTDPNKPLYLIHVACWWQNEADDATVYTMITKVLRRIKAEAKKRGKDSDYVYM
NYASLYEDVIRSYGKANQQRLQSIGKKYDPQAVFQKLQPGYFKLHKAPVTGSPYFTGQ

Enzyme Prediction     

EC	1.1.3.-:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	85	313	2.3e-51	0.4912663755458515

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	5.93e-11	96	232	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	9.65e-07	64	253	4	196	FAD/FMN-containing dehydrogenase [Energy production and conversion].
215242	PLN02441	0.008	215	253	193	231	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDR44461.1|AA7	4.34e-18	90	268	64	243
UQC87672.1|AA7	1.67e-17	96	514	70	489
APA09402.1|AA7|CBM18	1.76e-17	79	268	54	251
QRC92907.1|AA7	2.18e-17	103	266	69	235
QRW00715.1|AA7	2.89e-17	90	347	59	333

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	1.55e-25	96	515	45	454	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]
6FYG_A	2.81e-25	96	515	45	454	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]
6FYF_A	2.81e-25	96	515	45	454	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]
6FYE_A	3.79e-25	96	515	45	454	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
4XLO_A	5.10e-25	96	515	45	454	Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_B Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_C Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_D Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],6FOQ_A The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_B The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_C The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_D The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOW_A The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_B The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_C The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_D The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FP3_A The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_B The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_C The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_D The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FY8_A The crystal structure of EncM bromide soak [Streptomyces maritimus],6FY9_A The crystal structure of EncM complex with xenon under 15 bars Xe pressure [Streptomyces maritimus],6FYA_A The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus],6FYA_B The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|M2T7Z1|TPCD_COCH5	1.60e-88	86	525	69	518	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|A0A0U5GQ05|DRTC_ASPCI	8.22e-71	37	529	22	518	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|B6H064|PRX3_PENRW	1.20e-63	57	528	29	511	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
sp|W6Q5R7|PRX3_PENRF	1.20e-63	44	528	21	511	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1
sp|A0A023I4D6|PRX3_PENRO	1.20e-63	44	528	21	511	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000222	0.999747	CS pos: 18-19. Pr: 0.9803

TMHMM  Annotations     

There is no transmembrane helices in HMPREF1541_07107-t46_1-p1.