CAZyme Information: OTA36592.1

Basic Information

• Species: Hortaea werneckii
• Lineage: Ascomycota; Dothideomycetes; ; Teratosphaeriaceae; Hortaea; Hortaea werneckii
• CAZyme ID: OTA36592.1
• CAZy Family: GH92
• CAZyme Description: GMC_OxRdtase_N domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A1Z5TKL9]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
921	MUNK01000029|CGC2	102394.45	6.5125

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HwerneckiiEXF-2000	15649	1157616	29	15620

• Gene Location: location=MUNK01000029:255581-259861(-)

Full Sequence      

MAIHKGKRRKEDHLNMASTHMVAASGDEPAVVQILGFCKRNWFILLPLFIIIRFLYYRYS
SPLRHYPGPFLASGSRLWKVLSTYSGKTETDHILLHEKYSPTGCGRKLSRGSSEGKNNGG
SGGGGGNLVRIAPNELSLSSPLAAREVLAVGKGFHKTDFYAVFPPPENPDIFTETRESVH
AVKKRYASHAYSMSAMQQLSGCIEATERLLVEKLEGVASAGLREGEGKGGGVVDLGDYLH
YFAFDVLGEVAFSRKFGFLDAGADLEGAIKTIDEMQWYDGIVGQIPEWDWVFRRNPLWKL
VPGLDPARFLITRMAREEMEKRKRIGEKEVESGRKDLLSQLMAAHEKAPGQFGEGDVFAV
AHGAIFAGSDSTASTMQSFCHFVLSRPQVHARLKEEIDEASQGGRLSAMPQWNEVQALPY
FQACLKEAMRLRPAVGLNITRLTPPGGAEIDGQQIPGGVRIALNAWVLHRNEDVFGPDAK
VYKPERWLEDAEKAKAMERCMFQFGGGSHLCIGKNLALLEMNKLLPLLFRDFEMELVHPG
TELKYHSTFFVVQSGLETSFLEYAMKSSSLKVYPRAFTRQIIFDANKTATGITVQAGQTN
FTLNARKEVILSAGAFQSPQLLMVSGVGPENTLSQYNIPCVKHLPGVGQNMQDQPFFGID
YRVNVETSSMLVNDPQYHEDAVQKYLENATGPLANSPGFIAFERISQNQPSLLSNSTIEA
LNDNFPDDWPEAEYLVGNGYSGYNRNYRTADPGDGYNYAAIYSALISPFSKGNLTISSPD
MAVQPVINPNWLTDSRDKELAMAMFKRIRDIWANMRNVTIGEEYLPGPNVTTDEQIMEYI
QESVIQIYHAAATCKMGRSDDSMAVVDSRARVYGVKNLRVVDAAAFPFLTPGHPQSGVYM
LAEKIAEDIRLEREERIQTNY

Enzyme Prediction     

No EC number prediction in OTA36592.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA3	557	910	2.5e-110	0.6267605633802817

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
410683	CYP57A1-like	4.58e-172	128	557	3	424	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.
410684	CYP67-like	2.23e-88	129	543	4	400	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.
410682	CYP_fungal	3.68e-70	129	533	4	396	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.
410685	CYP58-like	6.31e-70	129	558	4	423	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.
410681	CYP60B-like	5.47e-66	129	537	4	396	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDS75323.1|AA3_2	1.29e-141	553	909	204	556
AMP40938.1|AA3_2	1.98e-139	557	911	203	555
QMW37598.1|AA3_2	2.34e-109	553	909	260	624
QMW25513.1|AA3_2	2.34e-109	553	909	260	624
QRD88504.1|AA3_2	2.34e-109	553	909	260	624

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2JBV_A	4.69e-30	553	913	207	530	Crystal structure of choline oxidase reveals insights into the catalytic mechanism [Arthrobacter globiformis],2JBV_B Crystal structure of choline oxidase reveals insights into the catalytic mechanism [Arthrobacter globiformis],4MJW_A Crystal Structure of Choline Oxidase in Complex with the Reaction Product Glycine Betaine [Arthrobacter globiformis],4MJW_B Crystal Structure of Choline Oxidase in Complex with the Reaction Product Glycine Betaine [Arthrobacter globiformis]
3NNE_A	4.69e-30	553	913	207	530	Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_B Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_C Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_D Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_E Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_F Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_G Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis],3NNE_H Crystal structure of choline oxidase S101A mutant [Arthrobacter globiformis]
6YS1_AAA	1.48e-29	608	906	260	557	Chain AAA, Fatty acid Photodecarboxylase [Chlorella variabilis]
3LJP_A	1.49e-29	553	913	207	530	Chain A, Choline oxidase [Arthrobacter globiformis],3LJP_B Chain B, Choline oxidase [Arthrobacter globiformis]
6YRU_AAA	1.97e-29	608	906	260	557	Chain AAA, Fatty acid Photodecarboxylase [Chlorella variabilis],6YRV_AAA Chain AAA, Fatty acid Photodecarboxylase [Chlorella variabilis],6YRX_AAA Chain AAA, Fatty acid Photodecarboxylase [Chlorella variabilis],6YRZ_AAA Chain AAA, Fatty acid photodecarboxylase, chloroplastic [Chlorella variabilis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A075TRK9|PATE_PENEN	5.55e-103	557	909	271	624	Patulin synthase OS=Penicillium expansum OX=27334 GN=patE PE=1 SV=1
sp|A1CFL2|PATE_ASPCL	1.15e-100	557	909	270	624	Patulin synthase OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=patE PE=1 SV=1
sp|Q5B8A1|PKFF_EMENI	8.99e-92	557	910	260	608	Dehydrogenase pkfF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=pkfF PE=2 SV=1
sp|Q12062|AFLK_ASPPU	7.23e-83	562	909	300	639	Versicolorin B synthase OS=Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) OX=1403190 GN=aflK PE=1 SV=1
sp|C8VDT4|STCN_EMENI	6.16e-80	527	909	269	635	Versicolorin B synthase stcN OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=stcN PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999992	0.000014

TMHMM  Annotations     

Start	End
42	61