P49602

PR
Gene name
ERG11 (CYP51, UMAG_03662)
Protein name
Lanosterol 14-alpha demethylase
Names
CYPLI, Cytochrome P450 51, Cytochrome P450-14DM, Cytochrome P450-LIA1, Sterol 14-alpha demethylase
Species
Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus)
KEGG Pathway
uma:UMAG_03662
EC number
1.14.14.154: With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

234-318 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P49602

Entry ID Method Resolution Chain Position Source
AF-P49602-F1 Predicted AlphaFoldDB

No variants for P49602

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P49602

No associated diseases with P49602

3 regional properties for P49602

Type Name Position InterPro Accession
domain F-box domain 565 - 609 IPR001810
domain Transcription elongation factor, TFIIS/CRSP70, N-terminal, sub-type 7 - 78 IPR003617
domain Transcription factor IIS, N-terminal 4 - 79 IPR017923

Functions

Description
EC Number 1.14.14.154 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
Subcellular Localization
  • Membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

5 GO annotations of molecular function

Name Definition
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
iron ion binding Binding to an iron (Fe) ion.
monooxygenase activity Catalysis of the incorporation of one atom from molecular oxygen into a compound and the reduction of the other atom of oxygen to water.
oxidoreductase activity Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
sterol 14-demethylase activity Catalysis of the reaction: a 14alpha-methyl steroid + 3 O2 + 3 reduced

2 GO annotations of biological process

Name Definition
ergosterol biosynthetic process The chemical reactions and pathways resulting in the formation of ergosterol, (22E)-ergosta-5,7,22-trien-3-beta-ol, a sterol found in ergot, yeast and moulds.
sterol metabolic process The chemical reactions and pathways involving sterols, steroids with one or more hydroxyl groups and a hydrocarbon side-chain in the molecule.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVASSSSATA SLLDQLFALT PLADSSAWIK TITVLVLLPL LAVVLNVASQ LLLATPKNHP
70 80 90 100 110 120
PVVFHFVPVI GSAIYYGIDP YKFFFECREK YGDVFTFVLL GRKITVALGP KGSNLVFNAK
130 140 150 160 170 180
HQQVTAEDAY THLTTPVFGK EVVYDVPNAV FMEQKKFVKV GLSIENFRVY VPQIVDEVRE
190 200 210 220 230 240
YIKSDARFSA LKTRKTITVD IFQAMSELII LTASRTLQGK EVRQGLDKSF AQLYHDLDSG
250 260 270 280 290 300
FTPINFVIPN LPLPSNFKRD RAQKKMSQFY QDIVAKRRAA GASTSADDAS GENDMIAALI
310 320 330 340 350 360
EQKYKNGRAL SGVEIAHMMI ALLMAGQHTS SATSSWAFLR LASRPEIIEE LYEEQLNVYS
370 380 390 400 410 420
DGHGGLRELD YETQKTSVPL LDAVVKETLR LHPPLHSIMR YVKSDLAVPP TLSSPTSTKS
430 440 450 460 470 480
EPDAHYVIPK GHYIMAAPGV SQVDPQIWKS SDQFDPHRWL DATTAAAMQD SGEDKQDFGF
490 500 510 520 530 540
GMISTGANSP YLPFGAGRHR CIGEQFAYLQ IGVILATFVR IFKWHLDSKF PDPDYQSMVV
550 560
LPSKNGCAIV LTPRAESLHL D