CAZyme Information: SPBR_05688-t41_1-p1

Basic Information

• Species: Sporothrix brasiliensis
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix brasiliensis
• CAZyme ID: SPBR_05688-t41_1-p1
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
716		76032.89	6.6655

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Sbrasiliensis5110	9231	1398154	140	9091

• Gene Location: location=AWTV01000004:1754751-1756901(+)

Full Sequence      

MAPFSTWTVLVGLLGLSASHVAHVAAVNFPWEAIQLTQSDVANFSAIRFGNNNDVSAARM
SRASCRAFPGTAAWPADAEWARLNATIDGALLRPQPAAAVCFAGPAYDATACRYLSRIAP
HTHYWLDTPLDVLTQWPEGNTCLVSLGTAPANKTNCTQGGYPEYVVNATTVKHIQAAVNF
ARNKNLRIVIKNTGHDFGGRSVGAGALSVWVHNLKSIEFLPRYRIGASVGAGAGSGASSS
SSREYDGMAVRYGAGVESWELFNHMGQHNISIAAPGGSTVGTLGGWLAMGGHGTVTSFLG
LGSDQALSIEVVTADGRLVTADPFHNTDLFFALRGGGPSTYGVMTSVVVKAFPPITMTSS
SVDIVFNADGPAAARPPLVFPGGSPPANGTGPFGFPNGTATANGSAPFPFAFPQPGTAAT
ADVFWAAVSKYYRFGQKVLDAGGMCFGYIYPRGNGSFSFTSSQFFANVTPERAHGMMQPL
FDDLATLGIRLTNPLPRFVSVYGAGHREGRGDGPVQTRYRSRLFPRANWADDALFNRTMA
AIRGSIEAGYTFHAIMHAPTYKTAGWPGRHSAVNPAWREALLHASLMETQPVGLTAHEAQ
ARDARAHAQIDTWRAVTPGSGAYMNEGDPTEPGWQQSFYGNLYPRLLAIKRRRDPWGLFW
APTTPGSEAWAVHTVDGYPGSQNGPLCRVASPVYGGGDDGEDGDDGDDDDDGDDDQ

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	158	359	3.4e-37	0.38427947598253276

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	1.52e-18	162	322	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	6.85e-13	160	353	30	205	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	1.02e-09	622	663	1	42	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	0.008	254	366	83	193	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	1.02e-53	43	670	474	1054
QKD57322.1|CBM91|GH43_11	1.02e-53	43	670	474	1054
BAI44126.1|AA7|CBM18	3.74e-15	162	662	275	713
QBZ61916.1|AA7|CBM18	3.74e-15	162	662	275	713
UQC87672.1|AA7	3.86e-15	162	374	70	258

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	2.27e-79	64	689	27	574	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	5.94e-51	65	688	30	597	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	8.04e-15	162	346	45	203	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYG_A	8.04e-15	162	346	45	203	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]
6FYB_A	1.42e-14	162	346	45	203	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|G2QDQ9|VAO15_MYCTT	1.17e-78	64	689	27	574	VAO-type flavoprotein oxidase VAO615 OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=MYCTH_2305637 PE=1 SV=1
sp|A0A1V6PBT1|CALF_PENDC	2.48e-75	63	689	25	575	Bifunctional decalin synthase calF OS=Penicillium decumbens OX=69771 GN=calF PE=1 SV=1
sp|A1CFM2|PATO_ASPCL	8.81e-74	64	689	28	568	FAD-linked oxidoreductase patO OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=patO PE=1 SV=1
sp|G0R6T3|SORD_HYPJQ	1.31e-69	61	690	35	574	FAD-linked oxidoreductase sor8 OS=Hypocrea jecorina (strain QM6a) OX=431241 GN=sor8 PE=3 SV=1
sp|A0A075TR33|PATO_PENEN	1.70e-69	64	689	27	567	FAD-linked oxidoreductase patO OS=Penicillium expansum OX=27334 GN=patO PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000228	0.999740	CS pos: 26-27. Pr: 0.4291

TMHMM  Annotations     

There is no transmembrane helices in SPBR_05688-t41_1-p1.