CAZyme Information: CPC735_070020-t26_1-p1

Basic Information

• Species: Coccidioides posadasii
• Lineage: Ascomycota; Eurotiomycetes; ; Onygenaceae; Coccidioides; Coccidioides posadasii
• CAZyme ID: CPC735_070020-t26_1-p1
• CAZy Family: GT62
• CAZyme Description: FAD binding domain containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
586	ACFW01000009|CGC6	65885.99	6.8541

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CposadasiiC735deltSOWgp	7255	222929	26	7229

• Gene Location: location=ACFW01000009:724002-725917(-)

Full Sequence      

MAAYSPLSPFSLALNEKENGMANEVLSTWQTTASRTPTLDILPPGVDAETWTGMLEEFKR
ILGDKGVLSGHEHRIRYIDPYAEKSDEQEKRGSSATLFPVTVEHIQAILKICNEHKIPLW
TVSRGKNLGYGGPAARVKGSIILDLQRMRKVIEVNDRYSYYTVEPGVTFFDIYRAIHAQK
KNIWCSVPALGWGSVVGNALDRGWGYTPAGDHSNQICGIEVVLADGTIVRTGAGAIDNSP
CWPLFRGGYGPTYESMFSQSNFGIVTKLTLWASPSPEGFMACRVDVESEDDLLPLIDGFR
DLLLHDVIQNHPLIGNLPREMVKRGQRKDFYDGKDAIPDARLKEIQKQFSIGFWSARFGL
YGPKEMVEFNYKRCQEVFDKLPGARLTGKAYYPPDGRKALSPEDIPLAERTVETGTPSLM
ALKAVEYRGKDGGHISFSPVLPPEGRCALSFYRDAKPLCARYGFDYFGGLHLYPRHLTMI
NMIYFDRTSDTERANASKLFVELVHLARKHGYSEYRAHIDYMDLVAEQYDFNGCSLRDLN
ERIKDALDPNGILSPGKQGIWPARYRQRKEEVSDMEKAVETLQLAN

Enzyme Prediction     

No EC number prediction in CPC735_070020-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA4	41	569	2.7e-164	0.9904214559386973

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	3.48e-33	57	558	1	455	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	9.31e-31	94	232	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.
397178	FAD-oxidase_C	3.98e-13	428	557	120	247	FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold.
183043	PRK11230	2.89e-10	44	292	14	244	glycolate oxidase subunit GlcD; Provisional
178402	PLN02805	2.59e-09	54	270	98	302	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QVM13434.1|AA4	0.0	1	586	1	586
CAE7177218.1|AA4	5.46e-158	37	566	27	560
QGA13141.1|AA4	7.49e-154	42	575	35	573
QRC93649.1|AA4	2.47e-153	37	567	26	560
BCS27721.1|AA4	3.39e-152	37	566	30	564

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5FXD_A	3.38e-116	42	566	5	522	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]
1W1L_A	9.00e-102	42	565	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]
1W1J_A	2.51e-101	42	565	12	553	STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: The505Ser Mutant [Penicillium simplicissimum],1W1J_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: The505Ser Mutant [Penicillium simplicissimum]
1E0Y_A	2.51e-101	42	565	12	553	Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1E0Y_B Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]
1DZN_A	2.51e-101	42	565	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|P56216|VAOX_PENSI	1.82e-100	42	565	12	553	Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
sp|P09788|DH4C_PSEPU	1.85e-99	41	560	8	515	4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
sp|F1QXM5|LDHD_DANRE	1.92e-15	54	281	35	252	Probable D-lactate dehydrogenase, mitochondrial OS=Danio rerio OX=7955 GN=ldhd PE=2 SV=1
sp|P94535|GLCD_BACSU	2.23e-14	81	277	29	218	Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
sp|D4MUV9|DLD_ANAHA	1.19e-12	54	299	13	246	D-lactate dehydrogenase OS=Anaerostipes hadrus OX=649756 GN=CL2_23160 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000075	0.000000

TMHMM  Annotations     

There is no transmembrane helices in CPC735_070020-t26_1-p1.