CAZyme Information: ASPVEDRAFT_123692-t33_1-p1

Basic Information

• Species: Aspergillus versicolor
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor
• CAZyme ID: ASPVEDRAFT_123692-t33_1-p1
• CAZy Family: AA3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
480		52887.26	4.4402

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AversicolorCBS583.65	13364	1036611	142	13222

• Gene Location: location=KV878126:2362612-2364163(-)

Full Sequence      

MRKLILSLALLALEAAAINLTAIYTNLSPGAEIVYTTDTDFRNETTPRYTIYRPPSSYGT
IIPATEADIQHIVQTSINNHIPFLATGAGHGITKTLGGFAFSDTGVTIQLSKFNAVEISP
DHEYITVGGGATYGEAYELMYNAGKMMAMGNSPCVGIVGAALGGAVGMWQGLYGLGIDAL
VSMRLVTATGELITVSATENPDLFWAIRGAGANFGIVTSATFRLHDVFNGGDVAMSFFRY
TADRNGSVWQALQGFDEDMPDLLAFNIAMSIGPEREPFIAVQANYYGPASEARAYIQPFH
DAAPFDVQERTLSWPDLQSYTHTVDPRNCAPGQYMNEWSISLKQTDINTYIEYYNQLHSL
WASEQRYTGQTVIARFPNRLARQVEDAATAYPHRSAVSHLLFENFYSDPELDDSINAWMP
EVMDLFQGTSGFDELHVYGNFAQGNEGPEAWYGGNLDRLKELKRVWDPNGLFNYNNPIPV

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	62	475	3.6e-58	0.9497816593886463

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	2.30e-33	61	473	36	451	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	1.82e-25	61	196	5	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.
369658	BBE	1.01e-08	437	479	1	45	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.
273751	FAD_lactone_ox	9.28e-08	63	229	21	183	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.
237553	murB	1.34e-07	61	225	35	190	UDP-N-acetylmuramate dehydrogenase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANF89368.1|AA7	8.32e-31	63	474	67	488
AEO58513.1|AA7|1.1.3.-	8.32e-31	63	474	67	488
QGI84728.1|AA7	2.82e-30	62	472	69	485
CCT71747.1|AA7	2.82e-30	62	472	69	485
QGI98385.1|AA7	2.82e-30	62	472	69	485

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	6.14e-38	87	479	75	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]
6FYG_A	8.46e-38	87	479	75	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]
6FYE_A	1.16e-37	87	479	75	460	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYF_A	1.60e-37	87	479	75	460	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]
6FYB_A	2.21e-37	87	479	75	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G3XMD0|AZAL_ASPNA	6.61e-111	4	463	6	471	FAD-linked oxidoreductase azaL OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaL PE=2 SV=2
sp|G3XMC1|AZAG_ASPNA	2.94e-108	26	465	30	468	FAD-linked oxidoreductase azaG OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaG PE=2 SV=1
sp|Q0CF74|AZPB3_ASPTN	5.47e-106	1	478	2	480	FAD-linked oxidoreductase ATEG_07660 OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=ATEG_07660 PE=1 SV=1
sp|Q5BEJ5|AFOF_EMENI	3.77e-100	1	479	1	479	FAD-linked oxidoreductase afoF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=afoF PE=1 SV=1
sp|Q7SHH8|SRDI_NEUCR	1.31e-85	46	480	63	497	FAD-linked oxidoreductase srdI OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=srdI PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000320	0.999661	CS pos: 17-18. Pr: 0.9702

TMHMM  Annotations     

There is no transmembrane helices in ASPVEDRAFT_123692-t33_1-p1.