CAZyme Information: OCF67589.1

Basic Information

• Species: Kwoniella mangrovensis
• Lineage: Basidiomycota; Tremellomycetes; ; Cryptococcaceae; Kwoniella; Kwoniella mangrovensis
• CAZyme ID: OCF67589.1
• CAZy Family: GH71
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
827		88856.92	5.3894

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_KmangroviensisCBS8507	8555	1296122	133	8422

• Gene Location: location=KI669476:654637-657598(-)

Full Sequence      

MAILNTTPNGSSAGIMTPEGLVKPYPFFAQPLKTPSNIAADDDLVKELREAVVEPTWQDI
PKPQVLGRNDDGFIASSTIFNGAVKTPALALVKPITAQDVSRTIVFCREHDLELSVKGGG
NGVHGWSVAGHIILDLSLMTDVTISLPDPSPPTLQESFQRLQVRRDSGTSTAGEPRRPSL
ASIHAASSDAGTKRSASDDFITDGTDDDGARRKGKVDGDRSGPYSPLDKIDEVIPAAEDS
RASSAMEQDNNGSGSRSNSGSGTRSGSASRSDSYGITGNGKDSTPATSISGTSEFTRSPK
SKSPIEDGYILPTHRFSFSSSNGSATSPEAGPSSRPGPRVTYVNPSQTPTSSFPFISTSF
GVNSSTSSSYSTSFHPSFASGPSTQLPLNTHPDPPPYTLVTFGAGVNSKALDAATAASPY
GAFHVPTSAFPVGAGQFISGGFGFIGRKHGLAMDNLVEVEMVLADGRIVWLGQDGKKGGG
WKDNEDPKEVWWAVRGAGAIIGVVTRFRAKAYYLPSVYAGNLIYLFDREKTPSLLRHVRD
CIKGSPRTLYTNIIMTAGPPGAPAIVVFQLCFSGARAEGEMYVQAISAWEGGRSLFQDFS
ERKFERQQLAVEEILKGGSGRKWFIKSDMLKSLSDEVIDETCSRFHSVPDGCTWLFEYTG
GGAITDVKDSCFPSSHRESAFTVAALHQWSHSESPVEDTRCVTTAEEWINEVIHPNSPGG
PLPCFLQSSLSSSVSAVYGESFPRLRALKKKLDPTNFFCHAMWPQNESEEDGINGLGEDI
KEGKIEGIQKEDIDKDGFMDEDELRERKKDDLEGKEKEKDKGKGKAL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	400	577	1.4e-23	0.3646288209606987

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	1.65e-09	400	472	66	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	4.79e-08	400	763	97	455	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	3.52e-06	88	142	1	56	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	9.84e-06	738	762	18	42	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.
223039	PHA03307	5.52e-04	140	352	120	350	transcriptional regulator ICP4; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UQC87672.1|AA7	2.53e-13	432	760	166	491
QRD93627.1|AA7	9.56e-13	399	758	113	464
QMW46638.1|AA7	9.56e-13	399	758	113	464
UDD63515.1|AA7	9.56e-13	399	758	113	464
CAK49173.1|AA7	1.57e-11	435	760	148	466

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYB_A	8.13e-25	435	758	143	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]
6FYF_A	1.45e-24	435	758	143	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	1.45e-24	435	758	143	453	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	1.45e-24	435	758	143	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	1.45e-24	435	758	143	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A2V5HCN7|PYVE_ASPV1	5.35e-18	435	758	136	443	FAD-linked oxidoreductase pyvE OS=Aspergillus violaceofuscus (strain CBS 115571) OX=1450538 GN=pyvE PE=3 SV=1
sp|Q54H55|Y8969_DICDI	1.69e-17	435	758	144	441	FAD-linked oxidoreductase DDB_G0289697 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0289697 PE=2 SV=1
sp|P08159|HDNO_PAENI	6.71e-14	435	760	136	449	(R)-6-hydroxynicotine oxidase OS=Paenarthrobacter nicotinovorans OX=29320 GN=6-hdno PE=1 SV=2
sp|I1SB12|MNCO_MICNN	1.37e-13	434	760	160	487	Carbohydrate oxidase OS=Microdochium nivale OX=5520 GN=MnCO PE=1 SV=2
sp|A6P6W1|CASL2_CANSA	2.00e-09	435	758	183	531	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 OTHER

Other	SP_Sec_SPI	CS Position
1.000073	0.000000

TMHMM  Annotations     

There is no transmembrane helices in OCF67589.1.