CAZyme Information: P170DRAFT_507141-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_507141-t37_1-p1
• CAZy Family: GT57
• CAZyme Description: FAD-binding domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
510		57268.46	4.9156

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsteyniiIBT23096	13430	1392250	235	13195

• Gene Location: location=MSFO01000002:2803361-2805129(+)

Full Sequence      

MKLVPQFLACGLALQQFVAGTPLPEYFDNTPITRCDLSVPKVGAELGRALSKGTMIFGPS
DSPWDEAVERYNTFVRPDIQIVVQPAEELDISTIVKYCNRNSIDFMVVNRGHAITSTIGT
FEGLQIDLSSLTNIDIAGDKKTAWFQGGTYDGQVMEVLWEKGYVATTGSCSCVGMMGPGL
GGGHGRYEGLYGLISDNLVNLNVVLADGSEIRVNNERHPDLFWAMQGAGHNFGIVTSFEL
KIYPRQVDSWHYHNYIWKQDQLETVFKELNKFHDNGNTPVLMGNNFGMYRMNATVSDNEA
ILYWTFAYAGPAKDGEELLKPFNAIPAVWDKQGDVPYPQISDIQGTGMKSPLCAPETTHI
TSTAGIKSYNITAQREIYELFNRRVAEQPEFKTARVVHEGYSNAGVRKRDPASSAFPFRD
ENHLLFFDAVLEEGSDLTEAAQEFAAEVRDLWNAGQPERKPSTYVNYAAGGEALESLYGW
EPWRLEWLRRLKARYDPHNRFRFYNPIITE

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	70	504	2.5e-59	0.980349344978166

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	1.37e-20	45	506	1	452	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	2.82e-19	80	214	2	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.
273751	FAD_lactone_ox	1.44e-05	84	244	20	180	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	0.006	463	507	1	44	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.
223882	MurB	0.007	70	246	11	184	UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADI58761.1|AA7|1.1.3.-	1.18e-20	46	501	3	464
AAS79317.1|AA7|1.1.3.-	3.37e-19	46	501	28	489
QRW09115.1|AA7	4.66e-19	51	244	47	243
QGI84728.1|AA7	7.90e-19	64	502	49	486
CCT71747.1|AA7	7.90e-19	64	502	49	486

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	6.85e-22	49	243	16	209	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	9.19e-22	49	243	16	209	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	1.23e-21	49	243	16	209	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYF_A	1.65e-21	49	243	16	209	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	1.65e-21	49	243	16	209	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|G4N287|OXR2_MAGO7	4.27e-195	1	507	1	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	1.13e-175	14	510	16	510	FAD-linked oxidoreductase iacH OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=iacH PE=1 SV=1
sp|G9N4A4|VIRI_HYPVG	4.75e-164	18	509	20	509	FAD-linked oxidoreductase virI OS=Hypocrea virens (strain Gv29-8 / FGSC 10586) OX=413071 GN=virI PE=3 SV=1
sp|B6HLP5|CHYH_PENRW	2.58e-69	18	507	9	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	1.15e-68	46	507	31	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000297	0.999676	CS pos: 20-21. Pr: 0.9671

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_507141-t37_1-p1.