CAZyme Information: CIHG_08818-t26_1-p1

Basic Information

• Species: Coccidioides immitis
• Lineage: Ascomycota; Eurotiomycetes; ; Onygenaceae; Coccidioides; Coccidioides immitis
• CAZyme ID: CIHG_08818-t26_1-p1
• CAZy Family: GT4
• CAZyme Description: flavoprotein subunit p-cresol methylhydroxylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
493		55288.79	6.1563

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CimmitisH538-4	10724	396776	186	10538

• Gene Location: location=DS017028:66377-68295(+)

Full Sequence      

MAAYSPLSPFSLALNEKENGMANEVLSTWQTTASRTPTLDILPPGVDAETWTGVLEEFKR
ILGDKGVLSGHEHRIRYIDPYAEESDEQEKRGSSATLFPVTVEHIQAILKICNEHKIPLW
TVSRGKNLGYEVTIFDIYRAIHAQKKNIWCSVPALGWGSVVGNALDRGWGYTPAGDHSNQ
ICGIEVVLADGTIVRTGAGAIDNSPCWPLFRGGYGPTYESMFSQSNFGIVTKLTLWASPS
PEGFMACRVDVESEDDLLPLIDGFRDLLLHDVIQNHPLIGNLPREMVKRGQRKDFYDGKD
AIPDARLKKIQKQFGIGFWSARFGLLMALKAVEYRGKDGGHISFSPVLPPEGSCALSFYR
DAKPLCARYGFDYFGGLHLYPRHLTMINMIYFDRTSDTERANASKLFVELVHLARKHGYS
EYRAHIDYMDLVAEQYDFNGCSLRDLNERIKDTLDPNGILSPGKQGIWPAQYRQQKEEVS
DMEKAVETLQLAN

Enzyme Prediction     

No EC number prediction in CIHG_08818-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA4	132	324	5.9e-65	0.367816091954023

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	8.33e-21	57	465	1	455	FAD/FMN-containing dehydrogenase [Energy production and conversion].
397178	FAD-oxidase_C	1.27e-14	318	464	107	247	FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold.
396238	FAD_binding_4	6.84e-14	94	197	2	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.
178402	PLN02805	5.21e-09	54	464	98	547	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QVM13434.1|AA4	0.0	1	493	1	586
CAE7177218.1|AA4	4.99e-109	37	473	27	560
QGA13141.1|AA4	3.21e-108	42	482	35	573
BCS27721.1|AA4	1.73e-104	37	473	30	564
QRC93649.1|AA4	1.79e-102	37	474	26	560

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5FXD_A	1.49e-76	42	475	5	524	Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXD_B Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXE_A Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXE_B Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXF_A Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXF_B Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXP_A Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1],5FXP_B Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1]
1WVE_A	2.21e-67	41	467	7	514	p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida],1WVE_B p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida],1WVF_A p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida]
1DII_A	2.26e-67	41	467	8	515	Chain A, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DII_B Chain B, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DIQ_A Chain A, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DIQ_B Chain B, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida]
1W1L_A	7.51e-67	42	472	12	553	STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum],1W1L_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum]
1DZN_A	2.05e-66	42	472	12	553	Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09788|DH4C_PSEPU	1.16e-66	41	467	8	515	4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
sp|P56216|VAOX_PENSI	1.47e-65	42	472	12	553	Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000068	0.000001

TMHMM  Annotations     

There is no transmembrane helices in CIHG_08818-t26_1-p1.