CAZyme Information: ASPCADRAFT_209242-t33_1-p1

Basic Information

• Species: Aspergillus carbonarius
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus carbonarius
• CAZyme ID: ASPCADRAFT_209242-t33_1-p1
• CAZy Family: GH32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
501		54644.45	5.1329

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=KV907503:1116157-1117722(+)

Full Sequence      

MEVVTAIAAWAFATASQLLPRSTDVHDLCSQQGDLKALGDRLSSTAKVYCPGSTGFTNAT
TRWSVLDEPEVNIVVVPGTENDVAEIVQFANQKDLPFLTYNGVHGALISLGEMTHGIAIY
MGQLSSVEVAEDGKTATIGGGTMSKVVTDELWAAGKQTVTGTCECVSLVGPALGGGHGWL
QGHHGLVLDQFVSMNIVLANGTLSTIDATSDLWWAVKGAGHNFGIVTSLTMKVYEIQHRD
WAIETLTFSGDKVQHVYQAANDYLVKNGTQPTGVINWSYWLNIADVDPTNPVIVFYIIQE
GVTTVDSTYTEPFHKIGPLAVEPNSGTYKDLAAWTEVAVTSAPCQKMGMANPRYPIYMES
YNVAAQQKAWAVYANATRGSSAFNNSIFMFEGYSVEGVHDIDSRSSAFAFRSENLLAAPL
INYYPNGTELDRRAANLGQELRNILFKGTGRDDIRAYVNYAHGDETPQQLYGSEKWRQQR
LRALKAKYDPTGKFSYYAPIP

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	59	494	1.5e-44	0.980349344978166

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	1.46e-20	73	207	3	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	5.28e-19	73	494	34	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	5.59e-07	456	501	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	2.23e-04	77	233	21	178	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
QRC92907.1|AA7	6.57e-22	37	271	28	267
CCA69005.1|AA7	2.83e-18	48	501	35	485
QGI84728.1|AA7	4.24e-18	52	494	45	485
CCT71747.1|AA7	4.24e-18	52	494	45	485
QGI98385.1|AA7	4.24e-18	52	494	45	485

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EO4_A	1.22e-22	38	501	5	469	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
6EO5_A	2.19e-22	38	501	5	469	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6FYG_A	9.04e-21	51	501	25	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]
6FYD_A	1.21e-20	51	501	25	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]
6FYE_A	2.17e-20	51	501	25	460	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|B6HLP5|CHYH_PENRW	1.25e-235	1	500	3	499	FAD-linked oxidoreductase chyH OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=chyH PE=3 SV=1
sp|I1S3L1|CHRY5_GIBZE	1.26e-210	1	500	3	505	FAD-linked oxidoreductase chry5 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=chry5 PE=3 SV=1
sp|G4N287|OXR2_MAGO7	3.77e-82	15	500	23	519	FAD-linked oxidoreductase OXR2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR2 PE=2 SV=1
sp|A0A1J0KJK5|IACH_PESFW	5.43e-79	38	500	49	507	FAD-linked oxidoreductase iacH OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=iacH PE=1 SV=1
sp|G9N4A4|VIRI_HYPVG	3.50e-75	14	500	21	507	FAD-linked oxidoreductase virI OS=Hypocrea virens (strain Gv29-8 / FGSC 10586) OX=413071 GN=virI PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.969822	0.030202

TMHMM  Annotations     

There is no transmembrane helices in ASPCADRAFT_209242-t33_1-p1.