CAZyme Information: Afu7g00940-T-p1

Basic Information

• Species: Aspergillus fumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fumigatus
• CAZyme ID: Afu7g00940-T-p1
• CAZy Family: GT15
• CAZyme Description: Has domain(s) with predicted UDP-N-acetylmuramate dehydrogenase activity, flavin adenine dinucleotide binding, oxidoreductase activity and role in oxidation-reduction process

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1039	Chr7_A_fumigatus_Af293|CGC17	111764.17	5.5928

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfumigatusAf293	10130	330879	290	9840

• Gene Location: location=Chr7_A_fumigatus_Af293:251118-254856(+)

Full Sequence      

MASSLKLSGIACLALLGSTVVAGKDSCSACSCSLTHFNATVGGRVQPLTPFSLPCFSSYN
GRPVARDDAACAAIQAKYTDPWLRTNSPNGYMNNQDEMWSSDPSDQCLLDSSDPTDPLAF
VNATCRQGNMPSHYLEVHSAKDVIEAFRYSNCSGQRLVIKNSGHDYLTRSSGRGTLALWT
RNLRSIRYDPAFVPSGCKRTGLKYKAITVGAGVNFDEAYAFAQQHNVTILGGYSSTVGLS
GGWVLNGGHSILSPVYGLGVDRVLEFKVVTPDGVFRTANEYQNADLFWALRGGGGGTFGV
VLESTHRVEPAVRFVSANINFPSTSSNMLPFMEIVVNNTLKWAQEGWGGHITGSTLVNVS
PLLTVEQAKASLAEVIAYAEANGGSASIEEFPSWYPFYEKYVTTSSVAVGVTRFPGSRLI
PRSVFETAEGRASLMDFFALLQSMGQTPYIPVVGPVLYNYTEGSTSAAPAWRQAVWELGS
GTSWAWNSTLPTRKQKIAGIQSMTAVIEGITPGSGAYSNEANPFTINWREAWWGENYERL
LRVKNKYDPRGLLKCWKCVGWEESDAATSPFAAASATLSMQSRNFTPPRKIEDCIQSPVK
MASFLAVAAYLTVIAAAHPLSTRLYPTVLRRDTTATSVEPVSAISLYYQAAANSSSIGAL
IQADLQLPSIVLEDVNDVSSVTCSVDSLTVTFNSTTTFNQAYSSWPRSHLLLVTNHLGNC
DAEADRGLYRAASLLFHPSTLTITASTRKTNLQQQAKTITIVFGHPDPSQHKRELATSID
LAWSGDLIRTNGLTIHANHATLDAAISIDGIIAYHVETRTATTLGLDIAVALDSSLGLSV
SAARPFLRNVYTYRWSPVEAAGFSIPGILTVGPILDLHVGVDMGMNGTAEAQSNMSMATN
GLFHLDLLNMTDSSARSVAPTATTSSRMDTAADMQLDPFVGAEVGVTVNLFEGLLDLSSG
LAARATVVNVFDVDAEVVVGADGDVTLVPPPTDANGGCENGYWMTSDFWFNVTASMTALV
TMDLYHLDMPLMQTRCIAF

Enzyme Prediction     

EC	1.1.3.-:1	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	137	326	1.3e-42	0.3799126637554585

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	6.67e-21	131	273	1	133	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	2.29e-15	111	553	12	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	6.84e-09	516	552	1	37	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	1.07e-05	117	291	8	162	UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis].
273751	FAD_lactone_ox	1.55e-05	128	329	12	197	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
QKD57322.1|GH43_11	1.31e-41	36	565	517	1055
QKD57322.1|CBM91|GH43_11	1.31e-41	36	565	517	1055
UPK90596.1|AA7	2.83e-13	131	552	20	434
QRW22693.1|AA7	4.23e-12	104	554	34	477
UNI23960.1|AA7	1.23e-11	139	311	56	217

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	3.90e-61	38	565	47	564	Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6F74_A	7.59e-41	37	563	48	586	Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_B Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_C Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_D Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6FYE_A	8.86e-18	139	554	53	454	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	2.08e-17	139	554	53	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]
6FYB_A	4.89e-17	139	554	53	454	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|A0A7L8UYL4|FFSJ_ASPFV	1.81e-152	38	562	30	589	FAD-linked oxidoreductase ffsJ OS=Aspergillus flavipes OX=41900 GN=ffsJ PE=3 SV=1
sp|G4MWA7|OXR2B_MAGO7	1.24e-136	41	563	36	565	FAD-linked oxidoreductase OXR2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR2 PE=2 SV=1
sp|P0CU32|CHEF_CHAGB	1.68e-136	41	570	76	604	FAD-linked oxidoreductase cheF OS=Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) OX=306901 GN=cheF PE=2 SV=1
sp|Q0V6Q5|PHMC_PHANO	9.13e-110	38	459	29	422	FAD-linked oxidoreductase phmC OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=phmC PE=3 SV=2
sp|D4AS41|A7056_ARTBC	9.55e-65	38	565	45	581	Uncharacterized FAD-linked oxidoreductase ARB_02478 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07056 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000217	0.999750	CS pos: 23-24. Pr: 0.6410

TMHMM  Annotations     

There is no transmembrane helices in Afu7g00940-T-p1.