CAZyme Information: OJD22650.1

Basic Information

• Species: Blastomyces percursus
• Lineage: Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Blastomyces; Blastomyces percursus
• CAZyme ID: OJD22650.1
• CAZy Family: GH2
• CAZyme Description: FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A1J9Q3I3]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
516	LGTZ01000995|CGC1	55812.39	7.3837

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BpercursusEI222	10384	N/A	99	10285

• Gene Location: location=LGTZ01000995:484-2208(+)

Full Sequence      

MFLAPLVAAAFLLLHSYVAAADVVTPAYKAATGFPPCDALIRAGLGNRLLLATDTGYEPR
IASWWSLNTRHRPWCLVKPHNAAEVSTAMTALLGAGAGNGAGDWHVAVRAGGHGPRLSNN
IDNGVTIDLGMLNQATYNKRTNLASIGPGGRWKDVLAKLLKYGVIVPSGRDGDVGVGGFL
LGGGSSYYMGREAFACDSVRNFEVVLTNGTIVNANKRENADLWRALKGGGSNFGIVTRFD
MDALPAKDIAYGTRFMSAEYSSELVDAIAHFTDHYQEFDTDALVAFLMHNTSAFPVDVVT
AAIHVNTEGIHNSTGFKKLNRIPSLIPDETRSLSLADAAEDSQLPSGTWNFGATITFKND
KRILAHAVKLHEKYVKDLNHDIGPENFVSLVLFQPEPSFLGDISKRRGGNMLGVDAQEHN
AILWTGGVAVKSDERALAIARTRMSAMVAELKEFSISLCGESRLIYMNYADPSQDPLGSY
GQENVDHIRRVAAKYDPLGVFQRRFPGGFKISRVGL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	63	502	6.4e-49	0.9781659388646288

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	3.62e-10	51	501	9	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	2.37e-07	73	215	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.
369658	BBE	0.006	466	501	2	38	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANH22765.1|AA7	3.14e-16	60	249	107	292
CCA70426.1|AA7	1.19e-15	53	501	73	509
ATZ50592.1|AA7	1.59e-15	35	262	24	256
QRD93627.1|AA7	1.77e-14	57	246	32	216
UDD63515.1|AA7	1.77e-14	57	246	32	216

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	1.85e-18	34	502	3	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	3.30e-18	34	502	3	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]
6FYF_A	3.30e-18	34	502	3	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]
6FYB_A	5.87e-18	34	502	3	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]
6FYE_A	5.87e-18	34	502	3	454	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A0U5GQ05|DRTC_ASPCI	7.76e-79	37	514	45	516	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|C8VPE5|SDCF_EMENI	2.55e-74	37	514	8	479	FAD-dependent monooxygenase sdcF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=sdcF PE=1 SV=1
sp|M2T7Z1|TPCD_COCH5	9.92e-55	53	512	51	518	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|D4B1P2|A2372_ARTBC	1.28e-47	14	512	1	500	Uncharacterized FAD-linked oxidoreductase ARB_02372 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02372 PE=1 SV=1
sp|G3Y424|YANF_ASPNA	4.28e-45	20	513	90	578	FAD-dependent monooxygenase yanF OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=yanF PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000572	0.999388	CS pos: 20-21. Pr: 0.9681

TMHMM  Annotations     

There is no transmembrane helices in OJD22650.1.