UniProtKB - M2PP75 (SIDA_CERS8)
L-ornithine N(5)-monooxygenase
SMO1
Functioni
L-ornithine N5-monooxygenase; part of the siderophore basidioferrin biosynthetic pathway (PubMed:28842536).
The biosynthesis of basidioferrin depends on the hydroxylation of ornithine to N5-hydroxyornithine, catalyzed by the monooxygenase SMO1 (PubMed:28842536).
The second step, the acylation of N5-hydroxy-L-ornithine is catalyzed by a not yet identified N-acyltransferase (PubMed:22434909).
Finally, assembly of basidioferrin is catalyzed by the nonribosomal peptide synthase (NRPS) NPS2 via amide bond formation between three L-AHO molecules to release the linear L-AHO trimer (PubMed:22434909).
1 PublicationCatalytic activityi
- EC:1.14.13.196By similarity
- EC:1.14.13.196By similarity
Cofactori
: Siderophore biosynthesis Pathwayi
This protein is involved in Siderophore biosynthesis.1 PublicationView all proteins of this organism that are known to be involved in Siderophore biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 69 | FAD; via amide nitrogenBy similarity | 1 | |
Binding sitei | 74 | SubstrateBy similarity | 1 | |
Binding sitei | 300 | SubstrateBy similarity | 1 | |
Binding sitei | 523 | SubstrateBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 50 – 58 | FADBy similarity | 9 | |
Nucleotide bindingi | 223 – 226 | NADPBy similarity | 4 | |
Nucleotide bindingi | 300 – 302 | NADPBy similarity | 3 | |
Nucleotide bindingi | 520 – 522 | FADBy similarity | 3 |
GO - Molecular functioni
- ornithine N5-monooxygenase activity Source: RHEA
Keywordsi
Molecular function | Monooxygenase, Oxidoreductase |
Ligand | FAD, Flavoprotein, NADP |
Names & Taxonomyi
Protein namesi | Recommended name: L-ornithine N(5)-monooxygenase1 Publication (EC:1.14.13.1961 Publication)Alternative name(s): Basidioferrin biosynthesis protein SMO11 Publication L-ornithine N(5)-oxygenaseCurated Siderophore biosynthesis protein SMO11 Publication |
Gene namesi | Name:SMO1 ORF Names:CERSUDRAFT_113443 |
Organismi | Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia subvermispora) |
Taxonomic identifieri | 914234 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Polyporales › Gelatoporiaceae › Gelatoporia › |
Proteomesi |
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PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000444313 | 1 – 541 | L-ornithine N(5)-monooxygenaseAdd BLAST | 541 |
Expressioni
Inductioni
Interactioni
Subunit structurei
Homotetramer.
By similarityProtein-protein interaction databases
STRINGi | 914234.M2PP75 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 269 – 272 | Substrate bindingBy similarity | 4 | |
Regioni | 430 – 474 | DisorderedSequence analysisAdd BLAST | 45 |
Sequence similaritiesi
Phylogenomic databases
HOGENOMi | CLU_020931_2_0_1 |
OrthoDBi | 1235295at2759 |
Family and domain databases
Gene3Di | 3.50.50.60, 1 hit |
InterProi | View protein in InterPro IPR036188, FAD/NAD-bd_sf IPR025700, Lys/Orn_oxygenase |
PANTHERi | PTHR42802, PTHR42802, 2 hits |
Pfami | View protein in Pfam PF13434, K_oxygenase, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MEAQDPLFDL IGLGFGPANL AIAGAIVEKW EGPSAGGDGG ISAHKVLFIE
60 70 80 90 100
KQPEFQWHPG MLLPNTRMQI SFLKDLATLR SPQSPLTFLS YLHAEGRLLP
110 120 130 140 150
FINRGSFTPT RREYFDYLSW AARTVESKGI KVQYGEEVVS IRGSEDNTVE
160 170 180 190 200
VHSRDVKTGT IVIRRTRNLV ISPGGNPKLP PNISLLYPHP RILHSSRYAT
210 220 230 240 250
SVDQLLGTLS PANRPLRIAV IGSGQSAAEV TLDLHSRLSS MPGGDRPHAI
260 270 280 290 300
DMIFRNGSLK PSDDSPFSNE IFDPDTTEVI YNLPTQSDRE NILKEYNNTN
310 320 330 340 350
YSVVNPRTID AMYEVMYDQK LDDAIARRKG DKATPSAARI TMHPHMTLYF
360 370 380 390 400
ADDLPQLAET DSATETSQEG IRLTLQNVFS QAQSTRDYDA VVCATGYDRT
410 420 430 440 450
SWLRMLTSSD IGKHFGLNLS SDPVQLVPST EIPKGPDGSL FDASEEEATW
460 470 480 490 500
RPASPITPAS PSPPSTPTSS ALSQSRMLGQ LPITKLYITR EYCLVPNSPQ
510 520 530 540
FKPRIYLQGC TEATHGLSES LLSILGVRAG LVVDDLWKNS Q
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | KB445795 Genomic DNA Translation: EMD38274.1 |
Genome annotation databases
EnsemblFungii | EMD38274; EMD38274; CERSUDRAFT_113443 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | KB445795 Genomic DNA Translation: EMD38274.1 |
3D structure databases
AlphaFoldDBi | M2PP75 |
SMRi | M2PP75 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 914234.M2PP75 |
Genome annotation databases
EnsemblFungii | EMD38274; EMD38274; CERSUDRAFT_113443 |
Phylogenomic databases
HOGENOMi | CLU_020931_2_0_1 |
OrthoDBi | 1235295at2759 |
Family and domain databases
Gene3Di | 3.50.50.60, 1 hit |
InterProi | View protein in InterPro IPR036188, FAD/NAD-bd_sf IPR025700, Lys/Orn_oxygenase |
PANTHERi | PTHR42802, PTHR42802, 2 hits |
Pfami | View protein in Pfam PF13434, K_oxygenase, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | SIDA_CERS8 | |
Accessioni | M2PP75Primary (citable) accession number: M2PP75 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 23, 2018 |
Last sequence update: | May 1, 2013 | |
Last modified: | May 25, 2022 | |
This is version 29 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families