CAZyme Information: EAQ86207.1

Basic Information

• Species: Chaetomium globosum
• Lineage: Ascomycota; Sordariomycetes; ; Chaetomiaceae; Chaetomium; Chaetomium globosum
• CAZyme ID: EAQ86207.1
• CAZy Family: CE3
• CAZyme Description: FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:Q2GX44]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
555		61050.02	6.8186

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CglobosumCBS148.51	11232	306901	184	11048

• Gene Location: location=CH408033:1970334-1972281(+)

Full Sequence      

MEALINAVEAQGVTVLKPGDKQYEYAVATENLMFRYLRPACVINAAIDTAQVQTVVREAQ
THKGHLTIKNGGHSYAGFSTTDGGILLDLSQMKNVTLDMTAGAETVTLQGGARWGHAYKK
LVDQRQDGLVVNGGRCPMVGVSGFVLGGGLSPCTRSFSMGCDTLLEATARATIVTADGSE
VTVTRHDENEDKRKLFWALCGAGCGNFGVVVELKMQLQKLASDNVVAGLFVWAPKPDPVA
MDAFMNTMVEFYTAEWPNKTTIDSSWVCNLEDARSELRVRFPIYHNAKQFKLRSAAESST
RFLLETLVSQWSFENQSTLSSATGRNEMAAFRGEFTGEEAFLQVTWIHTGGEANRDKTPE
TTAFPWRTCAYQTYVMLEWKEKWLTTSMKTFLRKMETELRKYSINSRAAFINFADGELQA
HEEAYFGTNAEALRKVKEKWDADFFFKSVQGVGLPPQLQIPHARTQGVSAQDGTTRVGQG
GSFVSESAYGDPGRGGSASMHASPAVRSGSTSVTKQFVERKDKPVNPMVDKMSMAETVRN
QFERGGSLSLLDFGF

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	40	248	2.6e-53	0.4148471615720524

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	4.63e-25	39	184	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.
223354	GlcD	2.50e-20	38	230	31	216	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	1.79e-10	409	453	1	45	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.
273751	FAD_lactone_ox	0.004	51	216	26	177	sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEO63154.1|AA7	1.76e-19	3	216	27	227
UPK94696.1|AA7	3.15e-18	2	452	27	489
AEO56694.1|AA7	1.03e-17	2	216	37	238
QBZ54840.1|AA7	1.81e-17	3	257	27	266
QGI68899.1|AA7	2.36e-16	4	225	28	236

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BVF_A	3.69e-21	35	240	34	224	Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVF_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVG_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVH_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans]
5I1V_A	1.13e-19	11	447	4	492	Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_A Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6]
4UD8_A	4.07e-19	35	452	73	527	AtBBE15 [Arabidopsis thaliana],4UD8_B AtBBE15 [Arabidopsis thaliana]
2Y08_A	1.68e-18	18	216	39	231	Structure of the substrate-free FAD-dependent tirandamycin oxidase TamL [Streptomyces sp. 307-9],2Y08_B Structure of the substrate-free FAD-dependent tirandamycin oxidase TamL [Streptomyces sp. 307-9],2Y3R_A Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_B Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_C Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_D Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3S_A Structure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group [Streptomyces sp. 307-9],2Y3S_B Structure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group [Streptomyces sp. 307-9],2Y4G_A Structure of the Tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P212121 space group [Streptomyces sp. 307-9],2Y4G_B Structure of the Tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P212121 space group [Streptomyces sp. 307-9]
1ZR6_A	8.39e-18	66	216	69	207	The crystal structure of an Acremonium strictum glucooligosaccharide oxidase reveals a novel flavinylation [Sarocladium strictum],2AXR_A Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD [Sarocladium strictum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9SA89|BBE12_ARATH	6.69e-23	38	456	76	530	Berberine bridge enzyme-like 12 OS=Arabidopsis thaliana OX=3702 GN=At1g30740 PE=2 SV=1
sp|Q796Y5|YGAK_BACSU	1.73e-21	24	456	17	444	Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4
sp|Q93ZA3|BBE13_ARATH	3.85e-21	23	459	63	534	Berberine bridge enzyme-like 13 OS=Arabidopsis thaliana OX=3702 GN=At1g30760 PE=1 SV=1
sp|P08159|HDNO_PAENI	1.89e-20	35	240	33	223	(R)-6-hydroxynicotine oxidase OS=Paenarthrobacter nicotinovorans OX=29320 GN=6-hdno PE=1 SV=2
sp|A0A0E0RTV6|ZEB1_GIBZE	4.32e-20	45	453	124	548	FAD-linked oxidoreductase ZEB1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=ZEB1 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000057	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EAQ86207.1.