CAZyme Information: KIW18440.1

Basic Information

• Species: Exophiala spinifera
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala spinifera
• CAZyme ID: KIW18440.1
• CAZy Family: GT1
• CAZyme Description: FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0D2BIN9]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
471		52811.59	6.2263

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EspiniferaCBS89968	12110	N/A	61	12049

• Gene Location: location=KN847493:1217271-1218686(+)

Full Sequence      

MGSTQESLPIIWRHETSEAEYEQATVGRVFNMRRPTRRPLAVVHAANESHIVTAVKLAIQ
QKCRVAVRSGGHSWAAWSVREDSILIDLGNYHHIELDEANHTVCVSPSTTGKTLNGLLKE
KGLMFAGGHCPDVGLGGFLLQGGMGWNCKNWGWACEQLFAIDAVNSQGELVHCNTTENSD
LFWCARGAGPGFPAVVTKFYLHVRPAPTHMLSTVLFYPLSKYHEVMEWVIKTSKGYDKDT
EIVSVAATPPAELGITQPCITPLFVTFKNSEEEAKAALKIANETRPAGALHELINHPTNL
AEQYKNQAEANPENHRYCAENAYISNDADVPAVLERAFTTLPTSKAFSLWYAMYPCSRRQ
LPDMALSMATDHYFALYTVWEDASDDARCRKWVKDIMTDVERHSDGSYLGDSDFQIRRTK
FWKSENGTRLMELRRKLDPTGLICGYLDEDDRSGTDGLPNQQEWRELHSSI

Enzyme Prediction     

No EC number prediction in KIW18440.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	28	442	3.4e-75	0.9759825327510917

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	3.45e-20	33	442	26	449	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	2.46e-19	39	174	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAI44126.1|AA7|CBM18	3.68e-26	25	212	262	449
QBZ61916.1|AA7|CBM18	3.68e-26	25	212	262	449
CBX96933.1|AA7|CBM18	1.07e-24	16	207	193	383
CAE7194773.1|AA7|CBM18	1.58e-23	16	212	115	310
QUC19098.1|AA7	2.40e-22	39	212	48	223

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	1.63e-27	10	443	22	453	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	4.08e-27	10	443	22	453	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]
6FYF_A	4.08e-27	10	443	22	453	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]
6FYE_A	5.54e-27	10	443	22	453	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYB_A	5.54e-27	10	443	22	453	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|A0A140JWT7|PTMO_PENSI	1.58e-97	8	448	9	443	FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|A0A0E3D8N6|PENO_PENCR	2.77e-95	7	448	8	443	FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|A0A2I6PJ02|NODO_HYPPI	1.15e-93	3	450	4	447	FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
sp|A0A0E3D8N0|JANO_PENJA	5.22e-92	8	447	6	443	FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
sp|G2QG48|XYLO_MYCTT	3.01e-22	8	212	36	236	Xylooligosaccharide oxidase OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=xylO PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000060	0.000000

TMHMM  Annotations     

There is no transmembrane helices in KIW18440.1.