CAZyme Information: ELR05098.1

Basic Information

• Species: Pseudogymnoascus destructans
• Lineage: Ascomycota; Leotiomycetes; ; Pseudeurotiaceae; Pseudogymnoascus; Pseudogymnoascus destructans
• CAZyme ID: ELR05098.1
• CAZy Family: GH18
• CAZyme Description: FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:L8FX91]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
720	GL573369|CGC1	79346.40	5.9829

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Pdestructans20631-21	9225	658429	150	9075

• Gene Location: location=GL573369:49258-52263(+)

Full Sequence      

MRSSTSFAAAIGILAAAPALADICQTLQASGRNVDKPFTLAYETEQKNYWSTACASLRPR
CMLSPNSTQEVADIVAALHKTNDQFAVKSGGHMPNNGFASIANGILISTRNLDQVVYDPD
TRNVVVGPGLKWEEIVKGIEETGRTVVGGRIGAVGVGGYLLGGGLSFLSAQYGWGANNVV
NYEIVLANATIVNANATSNQDLFASLKGGGNNFGIVTAFTIKTHPQAHKIWGGNYIIDAR
KTDQVLAAIRDFTEYNLDDKAAIIATSERSTLLNTWILFLFYDGLEPPAGVFDNFTHIGP
ILKTTKTRSYLELVKFNDQFILKGQRYVIATETTPLPNKTEGAVVMRSIYDHWTDVTKSI
ILEPGLLSSIAFQPMPRSITSKAKALGGDLMDFETTHDYIVMELDFSYLFASSDTAVDAA
TQNLYNGMRNIVDQHVENGRLPDIYRPLFMNDAYFREDYWGRLRTAEKARVFPFSRPRGA
EPAEEYAILRANEPVSKVELLDGSHAWLVVKHKDICSVLTDQRLSKQRNRPDFPELDQGG
KEAAKRKPTFVDMDKPDHMKQRGMIEDIFSREAIERMRPSIQNTVDTLLDDLIKDGCRNP
VDVVEKLALPVASYTIYGILGAPFEDLKFLTQQAAIRSNGSATATAASQANQDLLDYIGK
LVDMRVSEPNGDLISKIVTERIILTNILLLARDGPHPARQMAFLMLVAGNATMVNMINLD

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	48	267	3.7e-55	0.4781659388646288

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
410656	CYP105-like	1.08e-66	482	719	1	230	cytochrome P450 family 105 and similar cytochrome P450s. This group predominantly contains bacterial cytochrome P450s, including those belonging to families 105 (CYP105) and 165 (CYP165). Also included in this group are fungal family 55 proteins (CYP55). CYP105s are predominantly found in bacteria belonging to the phylum Actinobacteria and the order Actinomycetales, and are associated with a wide variety of pathways and processes, from steroid biotransformation to production of macrolide metabolites. CYP105A1 catalyzes two sequential hydroxylations of vitamin D3 with differing specificity and cytochrome P450-SOY (also known as CYP105D1) has been shown to be capable of both oxidation and dealkylation reactions. CYP105D6 and CYP105P1, from the filipin biosynthetic pathway, perform highly regio- and stereospecific hydroxylations. Other members of this group include, but are not limited to: CYP165D3 (also called OxyE) from the teicoplanin biosynthetic gene cluster of Actinoplanes teichomyceticus, which is responsible for the phenolic coupling of the aromatic side chains of the first and third peptide residues in the teicoplanin peptide; Micromonospora griseorubida cytochrome P450 MycCI that catalyzes hydroxylation at the C21 methyl group of mycinamicin VIII, the earliest macrolide form in the postpolyketide synthase tailoring pathway; and Fusarium oxysporum CYP55A1 (also called nitric oxide reductase cytochrome P450nor) that catalyzes an unusual reaction, the direct electron transfer from NAD(P)H to bound heme. The CYP105-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.
410657	Cyp158A-like	1.16e-39	482	717	1	226	cytochrome P450 family 158, subfamily A and similar cytochrome P450s. This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces coelicolor CYP158A1 and CYP158A2, Streptomyces natalensis PimD (also known as CYP107E), Mycobacterium tuberculosis CYP121, and Micromonospora griseorubida MycG (also known as CYP107B). CYP158A1 and CYP158A2 catalyze an unusual oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments; CYP158A2 produces three isomers of biflaviolin and one triflaviolin while CYP158A1 produces only two isomers of biflaviolin. PimD is a cytochrome P450 monooxygenase with native epoxidase activity that is critical in the biosynthesis of the polyene macrolide antibiotic pimaricin. CYP121 is essential for the viability of M. tuberculosis and is a novel drug target for the inhibition of mycobacterial growth. MycG catalyzes both hydroxylation and epoxidation reactions in the biosynthesis of the 16-membered ring macrolide antibiotic mycinamicin II. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.
410655	CYP107-like	1.38e-36	482	717	1	231	cytochrome P450 family 107 and similar cytochrome P450s. This group contains bacterial cytochrome P450s from families 107 (CYP107), 154 (CYP154), 197 (CYP197), and similar proteins. Among the members of this group are: Pseudonocardia autotrophica vitamin D(3) 25-hydroxylase (also known as CYP197A; EC 1.14.15.15) that catalyzes the hydroxylation of vitamin D(3) into 25-hydroxyvitamin D(3) and 1-alpha,25-dihydroxyvitamin D(3), its physiologically active forms; Saccharopolyspora erythraea CYP107A1, also called P450eryF or 6-deoxyerythronolide B hydroxylase (EC 1.14.15.35), that catalyzes the conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB; Bacillus megaterium CYP107DY1 that displays C6-hydroxylation activity towards mevastatin to produce pravastatin; Streptomyces coelicolor CYP154C1 that shows activity towards 12- and 14-membered ring macrolactones in vitro and may be involved in catalyzing the site-specific oxidation of the precursors to macrolide antibiotics, which introduces regiochemical diversity into the macrolide ring system; and Nocardia farcinica CYP154C5 that acts on steroids with regioselectivity and stereoselectivity, converting various pregnans and androstans to yield 16 alpha-hydroxylated steroid products. Bacillus subtilis CYP107H1 is not included in this group. The CYP107-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.
410700	CYP130-like	4.76e-27	486	717	4	229	cytochrome P450 family 130-like and similar cytochrome P450s. This subfamily includes Mycobacterium tuberculosis cytochrome P450 130 (CYP130), Rhodococcus erythropolis CYP116, and similar bacterial proteins. CYP130 catalyzes the N-demethylation of dextromethorphan, and has also shown a natural propensity to bind primary arylamines. CYP116 is involved in the degradation of thiocarbamate herbicides. The CYP130-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.
410659	CYP142-like	8.35e-27	486	712	1	224	cytochrome P450 family 142 and similar cytochrome P450s. This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces sp. P450sky (also called CYP163B3), Sphingopyxis macrogoltabida P450pyr hydroxylase, Novosphingobium aromaticivorans CYP108D1, Pseudomonas sp. cytochrome P450-Terp (P450terp), and Amycolatopsis balhimycina P450 OxyD, as well as several Mycobacterium proteins CYP124, CYP125, CYP126, and CYP142. P450sky is involved in the hydroxylation of three beta-hydroxylated amino acid precursors required for the biosynthesis of the cyclic depsipeptide skyllamycin. P450pyr hydroxylase is an active and selective catalyst for the regio- and stereo-selective hydroxylation at non-activated carbon atoms with a broad substrate range. P450terp catalyzes the hydroxylation of alpha-terpineol as part of its catabolic assimilation. OxyD is involved in beta-hydroxytyrosine formation during vancomycin biosynthesis. CYP124 is a methyl-branched lipid omega-hydroxylase while CYP142 is a cholesterol 27-oxidase with likely roles in host response modulation and cholesterol metabolism. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC92907.1|AA7	5.74e-22	58	253	62	262
QRD93627.1|AA7	1.20e-21	59	225	48	215
UDD63515.1|AA7	1.20e-21	59	225	48	215
QMW46638.1|AA7	3.82e-21	59	225	48	215
QGA17347.1|AA7	6.64e-21	27	226	14	217

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ULW_A	1.96e-85	466	719	1	249	Chain A, Cytochrome P450 55A1 [Fusarium oxysporum]
1XQD_A	2.02e-85	466	719	2	250	Chain A, CYTOCHROME P450 55A1 [Fusarium oxysporum]
1CMJ_A	1.06e-84	466	719	1	249	Chain A, CYTOCHROME P450 [Fusarium oxysporum]
1CL6_A	1.06e-84	466	719	1	249	Crystal Structures Of Ferric-No Complexes Of Fungal Nitric Oxide Reductase And Its Ser286 Mutants At Cryogenic Temperature [Fusarium oxysporum]
1CMN_A	1.06e-84	466	719	1	249	Chain A, CYTOCHROME P450 [Fusarium oxysporum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4B1P2|A2372_ARTBC	1.22e-159	23	469	28	476	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|Q12599|NOR2_FUSLI	7.11e-88	472	719	14	255	Cytochrome P450 55A3 OS=Fusarium lichenicola OX=42744 GN=CYP55A3 PE=3 SV=1
sp|Q00616|NOR1_FUSLI	9.75e-86	466	719	2	250	Cytochrome P450 55A2 OS=Fusarium lichenicola OX=42744 GN=CYP55A2 PE=3 SV=1
sp|P23295|NOR_FUSOX	5.60e-84	466	719	2	250	NADP nitrous oxide-forming nitric oxide reductase OS=Fusarium oxysporum OX=5507 GN=CYP55A1 PE=1 SV=2
sp|W6Q5R7|PRX3_PENRF	2.10e-48	50	389	59	403	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000474	0.999523	CS pos: 21-22. Pr: 0.9669

TMHMM  Annotations     

There is no transmembrane helices in ELR05098.1.