CAZyme Information: KFA56258.1

Basic Information

• Species: Stachybotrys chartarum
• Lineage: Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
• CAZyme ID: KFA56258.1
• CAZy Family: GT59
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
518		57794.81	4.4493

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: location=KL650235:268993-270851(-)

Full Sequence      

MGQLKFLAVCGLTLSSFLPQAVAAPHSCPDGLCLVTRTNVSNDQVSRELGPLLSCGAKIF
GPEDPNFAESTTRFQAFQPPNIELVVQVARERDVSTAISYADRNSLPFYVTNRRHGLAVS
QGSFTGIQIDVTQLQNITISEDGTYALFQGGTYDQQVIEYLWERGYVTTTGSCACVGMLG
PGLGGGHGRYQGLYGLISDNIRSLNVVLANGTEIYVSNTSHPDLYWGMQGAGHNFGAVTS
FELNIFPRLVDTWYFKNYLYTEDKLEELFERLNTLDNMGTQPAELMNFGFFHVNTEFNET
HLTSTKPLIWWSFSYAGPQADAEAYLGPFDSLGPINVTDGNVPYPEALHAVGTGLDDPMC
DHGVNHIVGTAGTQLYNITTQRAVFELFREKIAEYPGLVATYVVMEAYSLGAVLAKDPDS
SAFPMRDDYLLLQISANYLPDPSLDAPALEWAQQTIDLWNEGQPERRPTTYVNYGLGTES
LESIYGYEPWRLERLRDLKRRYDPYNKFRYYVPLIRDE

Enzyme Prediction     

EC	1.1.3.-:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	83	509	5.5e-45	0.9541484716157205

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	4.57e-14	83	214	2	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	5.25e-11	82	247	32	205	FAD/FMN-containing dehydrogenase [Energy production and conversion].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC92907.1|AA7	6.02e-20	32	508	13	484
UQC82080.1|AA7	1.33e-19	65	510	32	471
CCA69005.1|AA7	2.37e-19	56	510	32	480
QLI74064.1|AA7	6.63e-19	65	509	46	484
RDX44700.1|AA7|1.1.3.-	6.65e-17	127	504	116	500

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	4.30e-28	58	509	21	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]
6FYG_A	5.83e-28	58	509	21	454	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	7.90e-28	58	509	21	454	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYB_A	1.07e-27	58	509	21	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]
6FYF_A	1.07e-27	58	509	21	454	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G4N287|OXR2_MAGO7	3.73e-160	1	514	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	1.33e-150	34	518	34	511	FAD-linked oxidoreductase iacH OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=iacH PE=1 SV=1
sp|G9N4A4|VIRI_HYPVG	5.59e-141	40	515	39	508	FAD-linked oxidoreductase virI OS=Hypocrea virens (strain Gv29-8 / FGSC 10586) OX=413071 GN=virI PE=3 SV=1
sp|B6HLP5|CHYH_PENRW	4.67e-83	36	514	24	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	3.78e-79	36	514	18	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
0.000185	0.999794	CS pos: 23-24. Pr: 0.9782

TMHMM  Annotations     

There is no transmembrane helices in KFA56258.1.