CAZyme Information: ASPCADRAFT_208197-t33_1-p1

Basic Information

• Species: Aspergillus carbonarius
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus carbonarius
• CAZyme ID: ASPCADRAFT_208197-t33_1-p1
• CAZy Family: GH3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
529	KV907501|CGC5	56728.11	4.2919

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcarbonariusITEM5010	11735	602072	260	11475

• Gene Location: location=KV907501:263099-264902(+)

Full Sequence      

MLTGALLIAALAARATALDNTTSHIVAKLASYGVDAYEYFNSSVLLDSSLHSRSLGFCSE
LCSALPRLYPGHVLQRSTTAYSTWDASFWSQQQEEVDPACVFQPATTVEVAVGLLLTELT
LCPFAVKSGGHAAFSGASNIQDGLTIDLVSLNSTALSKDSTIASVGPGNRWVDVYEWLEP
KGLSVIGGRVSDIGVGGLTLGGGISFFSGIHGWACDNVANYEVVLADGSIVNVNLDTLPD
LYWALRGGGNNFGIVTRFDLTTHTQGLMWGGSRVWLENYQAAILQSLVNFGNDSPSDPNA
ALIVSVAYAEGLYLFVADLEYAKPVANPPIFDGFNSTGALEDTMAIRSLSNITLLFKEDN
PNGLRESYWTGTVQLDYELATNITNMFKQEIVPIQNVTGLVPALVWQVISTNTMEHMTKN
GGNALGLDATDGPLLLINLAFMWEDESDDAAVMAVLGSITAKALSAAKARGLGNDYLYMN
YASQYQSVVPSYGKANQARLQAISRKYDPLQVFEILQPGYFKLDGGLAL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	89	305	5.6e-52	0.4737991266375546

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	1.35e-16	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	6.77e-15	75	522	15	456	FAD/FMN-containing dehydrogenase [Energy production and conversion].
215242	PLN02441	3.54e-05	98	257	65	233	cytokinin dehydrogenase
273751	FAD_lactone_ox	0.004	98	255	15	171	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.
369658	BBE	0.005	478	513	2	38	Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANF89368.1|AA7	3.58e-21	73	313	38	286
AEO58513.1|AA7|1.1.3.-	3.58e-21	73	313	38	286
UNI23960.1|AA7	1.32e-20	96	263	46	215
CDR44461.1|AA7	3.07e-20	78	263	49	236
QRD93627.1|AA7	3.27e-20	96	263	46	214

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	8.68e-25	98	517	45	457	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	1.57e-24	98	517	45	457	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	1.57e-24	98	517	45	457	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]
4XLO_A	2.85e-24	98	517	45	457	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]
6FYE_A	2.85e-24	98	517	45	457	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|M2T7Z1|TPCD_COCH5	4.37e-107	33	524	5	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	7.23e-69	96	523	79	513	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|W6Q5R7|PRX3_PENRF	5.86e-68	42	523	17	507	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1
sp|A0A023I4D6|PRX3_PENRO	5.86e-68	42	523	17	507	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
sp|B6H064|PRX3_PENRW	2.24e-67	42	522	17	506	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
0.000418	0.999556	CS pos: 17-18. Pr: 0.9544

TMHMM  Annotations     

There is no transmembrane helices in ASPCADRAFT_208197-t33_1-p1.