CAZyme Information: P170DRAFT_435184-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_435184-t37_1-p1
• CAZy Family: GH3
• CAZyme Description: FAD-binding domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
535		58820.45	5.9815

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=MSFO01000003:20175-21782(-)

Full Sequence      

MRAPLVILALATTVCLGQETAARSSQAQDLYSCVSKVFSTTASQRIVRPEDDTYLDARLG
EKIQFTEFPLLIAYAEKAEEVGKLVKCAKKAGVKAVPRTGGHSFTAFSSLNGTLVIDIAH
INQVQVSRDRRSATVGAGIRLGALYTALNEYDTSFIGGICPTVGLAGFLGSGGFNMQQRS
QGLGVDHVLAAKVVTADGRTVLASPKSHPDLFWAIRGGGGGTYGIVVEFTLSLTKVPRSA
MLLLSWNNTEARFPVARRFLDWAPNQEPAFMSQINVYHDTVQVVAMHYGRSAQALRSIVN
ASGLLDIGHPEVVIAGGCNVDNARIFGYTAMDCLPDDQVDASILNVIPDPFSQVGNHPQF
QYKEERKSDTVGPAAPWDRFYRLSKSFFVQKNRPLSDEVLRGVVDRIGQLDEASEIWGEW
HSWNIPRKTLGSKNAFPWREQAYAHLEFQIHGSENQTQQQAYENWFEDLESFLRPAVGPA
SYSGYMDADISADPLVSYYGDNVCRLISIKQKYDPEEFFTNPFSIPASVPEGIEC

Enzyme Prediction     

EC	1.1.3.-:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	64	525	5.6e-75	0.9781659388646288

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	5.36e-28	69	201	1	136	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	9.47e-24	69	271	32	244	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	3.40e-10	481	526	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	4.76e-09	79	237	25	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.
178402	PLN02805	1.59e-05	69	287	134	353	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UJO23499.1|AA7	5.15e-30	69	529	63	487
AHG26149.1|AA7	1.83e-29	69	528	42	470
SAM83140.1|AA7	5.34e-29	12	525	30	539
UJO16207.1|AA7	2.88e-28	55	532	114	558
BAI44126.1|AA7|CBM18	9.75e-28	69	525	275	716

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EO5_A	9.52e-38	23	526	7	469	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6EO4_A	1.31e-37	23	526	7	469	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
3VTE_A	7.84e-37	28	530	5	515	Crystal structure of tetrahydrocannabinolic acid synthase from Cannabis sativa [Cannabis sativa]
6FYE_A	4.52e-31	38	236	14	211	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	1.14e-30	38	236	14	211	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q0CZH0|PYTB_ASPTN	5.32e-250	30	512	25	508	FAD-linked oxidoreductase pytB OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=pytB PE=2 SV=1
sp|A5ABH0|PYNB_ASPNC	6.94e-218	12	535	17	541	FAD-linked oxidoreductase pynB OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=pynB PE=1 SV=1
sp|Q8GTB6|THCAS_CANSA	5.58e-36	28	530	32	542	Tetrahydrocannabinolic acid synthase OS=Cannabis sativa OX=3483 GN=THCAS PE=1 SV=1
sp|A6P6W0|CASL1_CANSA	7.80e-34	28	526	32	538	Cannabidiolic acid synthase-like 1 OS=Cannabis sativa OX=3483 GN=CBDAS2 PE=2 SV=1
sp|A6P6W1|CASL2_CANSA	1.06e-33	28	526	32	538	Cannabidiolic acid synthase-like 2 OS=Cannabis sativa OX=3483 GN=CBDAS3 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000209	0.999779	CS pos: 17-18. Pr: 0.9762

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_435184-t37_1-p1.