dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: KFA50993.1

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Basic Information help

Species

Stachybotrys chartarum

Lineage

Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum

CAZyme ID

KFA50993.1

CAZy Family

GH154

CAZyme Description

unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
946	KL651400\|CGC1	104135.47	6.2526

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SchartarumIBT40293	11453	1280524	0	11453

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	1.1.3.-:1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA7	533	741	1.5e-48	0.45414847161572053

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	3.59e-25	533	663	5	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	2.76e-18	533	732	36	243	FAD/FMN-containing dehydrogenase [Energy production and conversion].
280596	Transferase	1.51e-16	23	452	34	431	Transferase family. This family includes a number of transferase enzymes. These include anthranilate N-hydroxycinnamoyl/benzoyltransferase that catalyzes the first committed reaction of phytoalexin biosynthesis. Deacetylvindoline 4-O-acetyltransferase EC:2.3.1.107 catalyzes the last step in vindoline biosynthesis is also a member of this family. The motif HXXXD is probably part of the active site. The family also includes trichothecene 3-O-acetyltransferase.
215266	PLN02481	8.54e-09	149	361	156	351	Omega-hydroxypalmitate O-feruloyl transferase
273751	FAD_lactone_ox	9.41e-08	519	707	5	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 help

Hit ID	E-Value	Query Start	Query End	Hit Start
4.28e-35	7	376	900	1256
5.64e-35	7	376	900	1256
3.90e-23	534	693	68	231
1.34e-21	534	742	169	384
1.37e-21	455	689	8	239

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.10e-54	13	461	17	458	Crystal Structure of F. sporotrichioides TRI101 complexed with Coenzyme A and T-2 [Fusarium sporotrichioides],2ZBA_B Crystal Structure of F. sporotrichioides TRI101 complexed with Coenzyme A and T-2 [Fusarium sporotrichioides],2ZBA_C Crystal Structure of F. sporotrichioides TRI101 complexed with Coenzyme A and T-2 [Fusarium sporotrichioides],2ZBA_D Crystal Structure of F. sporotrichioides TRI101 complexed with Coenzyme A and T-2 [Fusarium sporotrichioides]
9.49e-50	13	461	8	450	Chain A, Trichothecene 3-O-acetyltransferase [Fusarium graminearum],3B2S_A Chain A, Trichothecene 3-O-acetyltransferase [Fusarium graminearum],3B30_A Chain A, Trichothecene 3-O-acetyltransferase [Fusarium graminearum]
8.19e-47	13	461	9	451	Chain A, Trichothecene 3-O-acetyltransferase [Fusarium graminearum]
2.95e-27	512	940	23	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]
5.29e-27	512	940	23	460	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
3.80e-175	4	461	9	460	O-acetyltransferase epaC OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=epaC PE=3 SV=1
6.00e-174	4	461	9	460	O-acetyltransferase azaD OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaD PE=2 SV=1
2.50e-116	490	923	22	468	FAD-linked oxidoreductase azaG OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaG PE=2 SV=1
6.33e-114	490	924	22	471	FAD-linked oxidoreductase azaL OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaL PE=2 SV=2
2.01e-103	466	939	2	480	FAD-linked oxidoreductase ATEG_07660 OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=ATEG_07660 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000031	0.000000

TMHMM Annotations help

There is no transmembrane helices in KFA50993.1.