CAZyme Information: TPX39680.1

Basic Information

• Species: Synchytrium endobioticum
• Lineage: Chytridiomycota; Chytridiomycetes; ; Synchytriaceae; Synchytrium; Synchytrium endobioticum
• CAZyme ID: TPX39680.1
• CAZy Family: CE5
• CAZyme Description: beta-glucuronidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1084		121287.14	7.0757

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SendobioticumMB42	8031	N/A	0	8031

• Gene Location: location=QEAN01000343:2961-7411(-)

Full Sequence      

MKYRPNRYVCILLLSIASMVHTSQPQRLHVFDFTTPRPRPYRTNTISANYMGFSIEWNDM
QSLFTPTAQQIVFQLFSNLQSLSTKPLLIRVGGISEDEVWLVDSKFERNEKVFKFLIDAP
LLEGMTSLASQLSIEYLIGLPTMHSMRNVKATVEFAQALVDHGVINHTTGVELGNEPRNS
RISAADYARDYWIVMLEALYSSIPELQNLTFAGLSSYTPDEDIESHLDTITKGLSSFQNN
QVKTMLTAHTYGTYGHVSIQELLNTPTPQEFDYMHKVGKYGETHDVILGETNSVIGVGGG
VTAASNVFGSALWALDFYAYAAWKGLGSARLHGVMALENFTNIENDFHYSPFLINQDAET
AAKRPVNIRPLYYAMIAFTRALSFVSAAHDIIPIMPTNKTAPVTFIKVYGFSTAKGAKAS
FLIINKSNVLDMVSFNLPPNVHGEAVHIERLTAPSVSSTNGIAYAGQTFDGSVNGMPSGM
RVFEQVQVGPDGMYEIAVEAYSACVVLAGEGMELCGKDCSDNECIVSIHRQQEHGPVCDY
YSFITVERHLASPRSVSISQSISRRSRYYHLRTPQVMNPLTQLYARVRPIVPVAVLLLLL
ARYIGPGLYKFLRIYYHVSRLPGEISIGGFVRRGPAKGYRAFQEMHRKHRKKVVKIWPTT
ISVSDPKIVRELLMVRDIPKADMYQAFRFEFLPDHIFATSDRDFHKDIRRVLSPAFGIAY
LKSQETHILHAVDDLLAKWDGIIADTIDGPGLVNIWMDMHRVGTEVIGEIAFGTTFGTLR
NDSTAAALVENIEQGFRVGARMAFFPQALRKYPLIPIVKHSHQVSRNFIEMMTPVIYARR
NGTARKDILQCLIDGKWKDGTPLSDLHITVSALIMMFAGSDTSSNTMAFTIIHLLKNPHV
LERVVAEVLSVPLPAGQKLFTSNDVKTMMPYLEACIKESMRLTPVAIAVVRQADQDMVLH
GTEDTYFVPKGTTIILSSETLHNDPDTWKDPEVYQPERFLDAAAENEASTFSNISGNYMP
FSHGSRNCIGQHLALAEMRIVLANILKRYELYDVDPSQSREVSFQITLQLDSSSYIIGVQ
KRDA

Enzyme Prediction     

EC	3.2.1.166:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH79	48	333	1.8e-24	0.6725274725274726

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
410684	CYP67-like	2.80e-77	652	1051	2	391	cytochrome P450 family 67 and similar cytochrome P450s. This subfamily includes Uromyces viciae-fabae cytochrome P450 67 (CYP67), also called planta-induced rust protein 16, Cystobasidium minutum (Rhodotorula minuta) cytochrome P450rm, and other fungal cytochrome P450s. P450rm catalyzes the formation of isobutene and 4-hydroxylation of benzoate. The gene encoding CYP67 is a planta-induced gene that is expressed in haustoria and rust-infected leaves. The CYP67-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.
410651	cytochrome_P450	4.24e-74	653	1072	3	389	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.
395020	p450	2.73e-73	634	1051	11	433	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.
410683	CYP57A1-like	8.66e-70	652	1058	2	408	cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s. This family is composed of fungal cytochrome P450s including: Nectria haematococca cytochrome P450 57A1 (CYP57A1), also called pisatin demethylase, which detoxifies the phytoalexin pisatin; Penicillium aethiopicum P450 monooxygenase gsfF, also called griseofulvin synthesis protein F, which catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A during the biosynthesis of griseofulvin, a spirocyclic fungal natural product used to treat dermatophyte infections; and Penicillium aethiopicum P450 monooxygenase vrtE, also called viridicatumtoxin synthesis protein E, which catalyzes hydroxylation at C5 of the polyketide backbone during the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP57A1-like 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.
410677	CYP24A1-like	6.77e-67	649	1051	1	404	cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s. This family is composed of vertebrate cytochrome P450 24A1 (CYP24A1) and similar proteins including several Drosophila proteins such as CYP315A1 (also called protein shadow) and CYP314A1 (also called ecdysone 20-monooxygenase), and vertebrate CYP11 and CYP27 subfamilies. Both CYP314A1 and CYP315A1, which has ecdysteroid C2-hydroxylase activity, are involved in the metabolism of insect hormones. CYP24A1 and CYP27B1 have roles in calcium homeostasis and metabolism, and the regulation of vitamin D. CYP24A1 catabolizes calcitriol (1,25(OH)2D), the physiologically active vitamin D hormone, by catalyzing its hydroxylation, while CYP27B1 is a calcidiol 1-monooxygenase that coverts 25-hydroxyvitamin D3 to calcitriol. The CYP24A1-like 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
UQC88515.1|GT1	2.52e-42	653	1082	432	820
QKD56596.1|GH3	2.44e-34	653	1071	9	408
QHN99607.1|GT1	5.37e-17	839	1051	274	477
QHO55764.1|GT1	1.96e-16	875	1051	1	168
QKD46448.1|GH36	2.76e-15	641	1050	62	478

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7MK8_A	2.34e-33	637	1083	35	477	Chain A, Isoform 2 of Cytochrome P450 3A7 [Homo sapiens],7MK8_B Chain B, Isoform 2 of Cytochrome P450 3A7 [Homo sapiens]
5VCD_A	2.73e-33	637	1068	35	459	Crystal structure of the cysteine depleted CYP3A4 bound to glycerol [Homo sapiens],5VCE_A Crystal structure of the cysteine depleted CYP3A4 bound to ritonavir [Homo sapiens],5VCG_A Crystal structure of the cysteine depleted CYP3A4 bound to bromoergocryptine [Homo sapiens]
5VEU_A	1.54e-31	651	1076	45	461	Human Cytochrome P450 3A5 (CYP3A5) [Homo sapiens],5VEU_B Human Cytochrome P450 3A5 (CYP3A5) [Homo sapiens],5VEU_C Human Cytochrome P450 3A5 (CYP3A5) [Homo sapiens],5VEU_D Human Cytochrome P450 3A5 (CYP3A5) [Homo sapiens],5VEU_E Human Cytochrome P450 3A5 (CYP3A5) [Homo sapiens],5VEU_F Human Cytochrome P450 3A5 (CYP3A5) [Homo sapiens],5VEU_G Human Cytochrome P450 3A5 (CYP3A5) [Homo sapiens],5VEU_H Human Cytochrome P450 3A5 (CYP3A5) [Homo sapiens],5VEU_I Human Cytochrome P450 3A5 (CYP3A5) [Homo sapiens],5VEU_J Human Cytochrome P450 3A5 (CYP3A5) [Homo sapiens],5VEU_K Human Cytochrome P450 3A5 (CYP3A5) [Homo sapiens],5VEU_L Human Cytochrome P450 3A5 (CYP3A5) [Homo sapiens],6MJM_A Substrate Free Cytochrome P450 3A5 (CYP3A5) [Homo sapiens],7SV2_A Chain A, Cytochrome P450 3A5 [Homo sapiens],7SV2_B Chain B, Cytochrome P450 3A5 [Homo sapiens],7SV2_C Chain C, Cytochrome P450 3A5 [Homo sapiens],7SV2_D Chain D, Cytochrome P450 3A5 [Homo sapiens]
7LAD_A	1.56e-31	651	1076	46	462	Chain A, Cytochrome P450 3A5 [Homo sapiens]
7KVK_A	1.69e-31	637	1068	35	459	Chain A, Cytochrome P450 3A4 [Homo sapiens],7KVK_B Chain B, Cytochrome P450 3A4 [Homo sapiens],7KVS_A Chain A, Cytochrome P450 3A4 [Homo sapiens],7KVS_B Chain B, Cytochrome P450 3A4 [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1L9WQP6|ACRD_ASPA1	1.91e-51	598	1082	24	500	Cytochrome P450 monooxygenase acrD OS=Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094) OX=690307 GN=acrD PE=2 SV=1
sp|W7MLD1|FUS8_GIBM7	1.29e-49	606	1082	45	513	Cytochrome P450 monooxygenase FUS8 OS=Gibberella moniliformis (strain M3125 / FGSC 7600) OX=334819 GN=FUS8 PE=3 SV=1
sp|S0EE84|FUS8_GIBF5	2.64e-48	604	1082	43	513	Cytochrome P450 monooxygenase FUS8 OS=Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) OX=1279085 GN=FUS8 PE=1 SV=1
sp|A0A6J4BC30|LUC2_FUSSX	5.93e-45	643	1082	87	509	Cytochrome P450 monooxygenase LUC2 OS=Fusarium sp. OX=29916 GN=LUC2 PE=3 SV=1
sp|A0A0D1DT62|CYP2_USTMA	2.01e-42	639	1084	75	532	Cytochrome P450 monooxygenase cayp2 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=cyp2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000212	0.999758	CS pos: 25-26. Pr: 0.9402

TMHMM  Annotations     

There is no transmembrane helices in TPX39680.1.