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CAZyme Information: P175DRAFT_0472569-t39_1-p1

You are here: Home > Sequence: P175DRAFT_0472569-t39_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Aspergillus ochraceoroseus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus ochraceoroseus
CAZyme ID P175DRAFT_0472569-t39_1-p1
CAZy Family GH154
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
787 89068.87 7.0218
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AochraceoroseusIBT24754 9070 1392256 153 8917
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in P175DRAFT_0472569-t39_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT34 66 257 5e-28 0.8861788617886179

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
410682 CYP_fungal 3.99e-111 435 787 1 343
unknown subfamily of fungal cytochrome P450s. This subfamily is composed of uncharacterized fungal cytochrome P450s. 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 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.
410684 CYP67-like 5.81e-80 435 786 1 337
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.
410681 CYP60B-like 5.27e-71 435 787 1 338
cytochrome P450 family 60, subfamily B and similar cytochrome P450s. This family is composed of fungal cytochrome P450s including: Aspergillus nidulans cytochrome P450 60B (CYP60B), also called versicolorin B desaturase, which catalyzes the conversion of versicolorin B to versicolorin A during sterigmatocystin biosynthesis; Fusarium sporotrichioides cytochrome P450 65A1 (CYP65A1), also called isotrichodermin C-15 hydroxylase, which catalyzes the hydroxylation at C-15 of isotricodermin in trichothecene biosynthesis; and Penicillium aethiopicum P450 monooxygenase vrtK, also called viridicatumtoxin synthesis protein K, which catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to produce viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP60B-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.
410685 CYP58-like 5.68e-69 435 787 1 346
cytochrome P450 family 58-like fungal cytochrome P450s. This group includes Fusarium sporotrichioides cytochrome P450 58 (CYP58, also known as Tri4 and trichodiene oxygenase), and similar fungal proteins. CYP58 catalyzes the oxygenation of trichodiene during the biosynthesis of trichothecenes, which are sesquiterpenoid toxins that act by inhibiting protein biosynthesis. The CYP58-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.
410683 CYP57A1-like 1.56e-67 435 787 1 352
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 7 787 5 790
5.03e-144 8 354 10 357
1.37e-125 6 349 3 349
6.01e-124 51 351 28 326
2.53e-121 51 351 45 342

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.37e-14 478 787 95 393
Human CYP3A4 bound to an inhibitor fluconazole [Homo sapiens]
1.81e-14 391 787 5 393
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]
5.51e-14 478 787 92 390
Crystal structure of CYP3A4 in complex with an inhibitor [Homo sapiens]
5.53e-14 478 787 93 391
Crystal structure of human cytochrome P450 3A4 [Homo sapiens],1W0F_A Crystal structure of human cytochrome P450 3A4 [Homo sapiens],1W0G_A Crystal structure of human cytochrome P450 3A4 [Homo sapiens],2J0D_A Crystal structure of human P450 3A4 in complex with erythromycin [Homo sapiens],2J0D_B Crystal structure of human P450 3A4 in complex with erythromycin [Homo sapiens],2V0M_A Crystal structure of human P450 3A4 in complex with ketoconazole [Homo sapiens],2V0M_B Crystal structure of human P450 3A4 in complex with ketoconazole [Homo sapiens],2V0M_C Crystal structure of human P450 3A4 in complex with ketoconazole [Homo sapiens],2V0M_D Crystal structure of human P450 3A4 in complex with ketoconazole [Homo sapiens],3NXU_A Crystal structure of human cytochrome P4503A4 bound to an inhibitor ritonavir [Homo sapiens],3NXU_B Crystal structure of human cytochrome P4503A4 bound to an inhibitor ritonavir [Homo sapiens]
5.55e-14 478 787 94 392
Crystal Structure of Human Microsomal P450 3A4 [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.48e-98 388 787 25 405
Cytochrome P450 monooxygenase orf2 OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=orf2 PE=3 SV=1
1.02e-82 435 787 30 363
Cytochrome P450 monooxygenase azaI OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaI PE=2 SV=1
5.47e-57 394 786 56 430
Cytochrome P450 monooxygenase stcB OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=stcB PE=2 SV=2
2.82e-54 379 786 30 421
Cytochrome P450 monooxygenase cypX OS=Dothistroma septosporum (strain NZE10 / CBS 128990) OX=675120 GN=cypX PE=2 SV=1
2.82e-54 379 786 30 421
Cytochrome P450 monooxygenase cypX OS=Dothistroma septosporum OX=64363 GN=cypX PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.966815 0.033209

TMHMM  Annotations      download full data without filtering help

Start End
12 31