CAZyme Information: PWY81892.1

Basic Information

• Species: Aspergillus heteromorphus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus heteromorphus
• CAZyme ID: PWY81892.1
• CAZy Family: GH3
• CAZyme Description: FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A317W9G3]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1101	MSFL01000013|CGC2	121976.90	7.3134

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AheteromorphusCBS117.55	11436	1448321	306	11130

• Gene Location: location=MSFL01000013:345752-354424(-)

Full Sequence      

MALTMYLILALAAVLVLHSFLSSRKLQRQRGLPHIPLVKFDRDDTQANYVMRTKEIMHQG
YLKYTKNGIAFRIRNPIDEGSPQVIIPSKYLDEVKNAPETELSFPLHAIQSFLLEYSGSA
LPSLAATNVTRIDLNKNLGELVGGLKEECLDALGTVIPESTDWTPLKPWEVSLPLVARMT
GRVLVGPKLCSDPEWIQLTIANTTGIMKSAMEIRASYSARWQWLAPWTYRRRKDLLTLRK
RAARMIEPLYRERIATNSHTEKHRDAVQWLIDNGNHDGQVTSPAEIADGLLFLYMAGIHS
TSATVVSMMYDLIAHSDYIPELLEEIHQVLADSPEWSKQSLAKLRKLDSFMKESQRLHPV
GHVTVQRSTVKPFTFHDGVRLPANTHLSFPTDELTHDPDVYPQPDVFDGLRFYHMRRDGD
ASKFHFATVSNQSTNFGAGFHACPGRFLHAPAHYFQSRGARFRSGNVRTESQDAMSSGTT
VMRVCVLGVAASIRCLAAAPLAGSRTARINAPIWGMRENRHSHHISSQWNWATLNATLHG
RLQGTVPLARPCFDSYDGRLAMFQPSQCSEVQAQYTSAAYRADLYSGFMHAQNEICAAST
DQLTRQCLLGPTEPLVDPPSTSCGQGSVSHYHIPVTDAADVQAAFAFARQTGVTLSIKNS
GHDYSGRSSLRGSLALWTRPMQQLIYHPNDFVPAGCSAQHRAAHAITVGAGVNFDQVYRF
AHEHNVTFIGGTAPTVGVSGGFAMTGGHGLLTAQFGLGIDRVLEYKIVTADGELRTANAC
QHQDLFWALRGGGGATYGVVVESTHRVEPSRPLVFASLTLPAPDANFTRLLIRHARRWSL
QGWGGPNAMDRIAMANPFLDLPAARASLAEVIDYVDAHDGGSVSLTVYPDFYPIYQEYMT
ATADAGVGTASFATNRLIPTTLFQQPNDTARLLDELVLLAAEGYAPTLFATPPAYYESRQ
PSNPPPPTTTTNHNDDDNNNNNNTSTTPAWRDSTWMITVSAEWAWNSTLAEKRAFVRNFQ
SVTQRLARLAPRSGAYISEADPFTPDWRTAWWGDENYAHLLRIKRKYDPAGLLRCWRCVG
WEEERADPDGGFGCLGGLVDV

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	635	1076	1.2e-56	0.9475982532751092

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
410667	CYP503A1-like	1.03e-127	58	448	1	391	cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s. This family is composed of predominantly fungal cytochrome P450s (CYPs) with similarity to Fusarium fujikuroi Cytochrome P450 503A1 (CYP503A1, also called ent-kaurene oxidase or cytochrome P450-4), Aspergillus nidulans austinol synthesis protein I (ausI), Alternaria alternata tentoxin synthesis protein 1 (TES1), and Acanthamoeba polyphaga mimivirus cytochrome P450 51 (CYP51, also called P450-LIA1 or sterol 14-alpha demethylase). Ent-kaurene oxidase catalyzes three successive oxidations of the 4-methyl group of ent-kaurene to form kaurenoic acid, an intermediate in gibberellin biosynthesis. AusI and TES1 are cytochrome P450 monooxygenases that mediate the biosynthesis of the meroterpenoids, austinol and dehydroaustinol, and the phytotoxin tentoxin, respectively. P450-LIA1 catalyzes the 14-alpha demethylation of obtusifoliol and functions in steroid biosynthesis. 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.
410651	cytochrome_P450	6.68e-28	170	448	105	350	cytochrome P450 (CYP) superfamily. Cytochrome P450 (P450, CYP) is a large 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 with > 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. 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. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis.
410668	CYP51-like	1.58e-27	223	445	151	367	cytochrome P450 family 51 and similar cytochrome P450s. This family is composed of cytochrome P450 51 (CYP51 or sterol 14alpha-demethylase) and related cytochrome P450s. CYP51 is the only cytochrome P450 enzyme with a conserved function across animals, fungi, and plants, in the synthesis of essential sterols. In mammals, it is expressed in many different tissues, with highest expression in testis, ovary, adrenal gland, prostate, liver, kidney, and lung. In fungi, CYP51 is a significant drug target for treatment of human protozoan infections. In plants, it functions within a specialized defense-related metabolic pathway. CYP51 is also found in several bacterial species. 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.
395020	p450	2.45e-26	222	448	199	415	Cytochrome P450. Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.
396238	FAD_binding_4	2.60e-23	635	778	7	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD57322.1|GH43_11	1.68e-30	523	1080	507	1050
QKD57322.1|CBM91|GH43_11	1.68e-30	523	1080	507	1050
QBZ61175.1|AA3_2	8.07e-22	9	450	15	474
QUC19098.1|AA7	8.00e-13	588	809	4	216
CCA72155.1|AA7	1.40e-12	702	886	172	350

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	7.72e-56	527	1090	39	569	Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6F74_A	1.39e-42	531	1090	45	593	Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_B Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_C Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_D Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6EO5_A	1.44e-18	636	844	55	246	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6EO4_A	1.44e-18	636	844	55	246	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
6FYE_A	2.26e-17	636	811	52	215	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G4MWA7|OXR2B_MAGO7	2.73e-145	530	1096	28	578	FAD-linked oxidoreductase OXR2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR2 PE=2 SV=1
sp|A0A7L8UYL4|FFSJ_ASPFV	5.00e-145	522	1099	17	614	FAD-linked oxidoreductase ffsJ OS=Aspergillus flavipes OX=41900 GN=ffsJ PE=3 SV=1
sp|P0CU32|CHEF_CHAGB	1.01e-134	530	1099	68	616	FAD-linked oxidoreductase cheF OS=Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) OX=306901 GN=cheF PE=2 SV=1
sp|A1CLZ3|CCSG_ASPCL	1.17e-113	1	448	1	448	Cytochrome P450 monooxygenase ccsG OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=ccsG PE=3 SV=1
sp|Q0V6Q5|PHMC_PHANO	1.15e-104	530	956	24	421	FAD-linked oxidoreductase phmC OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=phmC PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000062	0.000000

TMHMM  Annotations     

Start	End
5	22