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UniProtKB - Q2TZB2 (SIDA_ASPOR)
Protein
L-ornithine N(5)-monooxygenase
Gene
dffA
Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Functioni
Catalyzes the conversion of L-ornithine to N5-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as deferriferrichrysin.
1 PublicationCatalytic activityi
- EC:1.14.13.1961 Publication
- EC:1.14.13.1961 Publication
Cofactori
FADBy similarityNote: Binds 1 FAD per subunit.By similarity
: 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 | 102 | FAD; via amide nitrogenBy similarity | 1 | |
Binding sitei | 107 | SubstrateBy similarity | 1 | |
Binding sitei | 168 | FAD; via amide nitrogen and carbonyl oxygenBy similarity | 1 | |
Binding sitei | 279 | NADPBy similarity | 1 | |
Binding sitei | 323 | SubstrateBy similarity | 1 | |
Binding sitei | 469 | SubstrateBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 83 – 91 | FADBy similarity | 9 | |
Nucleotide bindingi | 254 – 257 | NADPBy similarity | 4 | |
Nucleotide bindingi | 323 – 325 | NADPBy similarity | 3 | |
Nucleotide bindingi | 466 – 468 | FADBy similarity | 3 |
GO - Molecular functioni
- N,N-dimethylaniline monooxygenase activity Source: AspGD
- ornithine N5-monooxygenase activity Source: RHEA
GO - Biological processi
- cellular response to iron ion starvation Source: EnsemblFungi
- ferrichrome biosynthetic process Source: EnsemblFungi
- siderophore biosynthetic process Source: AspGD
Keywordsi
Molecular function | Monooxygenase, Oxidoreductase |
Ligand | FAD, Flavoprotein, NADP |
Names & Taxonomyi
Protein namesi | Recommended name: L-ornithine N(5)-monooxygenaseBy similarity (EC:1.14.13.1961 Publication)Short name: OMOBy similarity Alternative name(s): Deferriferrichrysin biosynthesis protein A1 Publication L-ornithine N(5)-oxygenase1 Publication |
Gene namesi | Name:dffA1 Publication ORF Names:AO090011000926 |
Organismi | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
Taxonomic identifieri | 510516 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Circumdati › |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | FungiDB:AO090011000926 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000431071 | 1 – 502 | L-ornithine N(5)-monooxygenaseAdd BLAST | 502 |
Proteomic databases
PRIDEi | Q2TZB2 |
Expressioni
Inductioni
Induced under iron-limiting conditions.1 Publication
Interactioni
Subunit structurei
Homotetramer.
By similarityProtein-protein interaction databases
STRINGi | 510516.Q2TZB2 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 34 | DisorderedSequence analysisAdd BLAST | 34 | |
Regioni | 293 – 296 | Substrate bindingBy similarity | 4 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 15 – 29 | Polar residuesSequence analysisAdd BLAST | 15 |
Sequence similaritiesi
Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.Curated
Phylogenomic databases
OMAi | YHGNTNY |
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, 1 hit |
Pfami | View protein in Pfam PF13434, K_oxygenase, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit |
i Sequence
Sequence statusi: Complete.
Q2TZB2-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MEPVERKLEI GSRSYSKMPL TQQRSSGEPP RLKATPKDEL HDLLCVGFGP
60 70 80 90 100
ASLAIAIALH DALDPCLNKT PNSNWQPKVC FLERQKQFAW HSGMLVPGSK
110 120 130 140 150
MQISFIKDLA TMRDPRSSFT FLNYLHQKDR LIHFTNLSTF LPARMEFEDY
160 170 180 190 200
MRWCAQRFAH VVSYGEEVIE VIPGKTNPSS TLVDFFTVKS RNVETGEISA
210 220 230 240 250
RMARKVVVAL GGTAKLPKEL PQDPRIMHSS KYCTTLPAML KDSREAYNIA
260 270 280 290 300
VLGSGQSAAE IFHDLQKRYP NSKTTLIMRD TAMRPSDDSP FVNEVFNPER
310 320 330 340 350
VDKFFSLSSA ERQRSLTADK ATNYSVVRLE LIEQIFNDMY LQRVQNPDET
360 370 380 390 400
QWQHRILPGR KITRVEHYGP HRRMRLHVRA VKDEKDSLVG NGKETLEVDA
410 420 430 440 450
LMVATGYNRN AHEQLLKNVQ HLRPAGQENW TPNREYRVEL DPSKVNAQAG
460 470 480 490 500
IWLQGCNEQT HGLSDSLLSI LASRSGEMVN SIFGGEFAGT TVPDTTHIRA
ML
Sequence cautioni
The sequence BAE65353 differs from that shown. Reason: Erroneous gene model prediction.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB071287 Genomic DNA Translation: BAC15565.1 AP007171 Genomic DNA Translation: BAE65353.1 Sequence problems. |
RefSeqi | XP_001826486.2, XM_001826434.2 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB071287 Genomic DNA Translation: BAC15565.1 AP007171 Genomic DNA Translation: BAE65353.1 Sequence problems. |
RefSeqi | XP_001826486.2, XM_001826434.2 |
3D structure databases
AlphaFoldDBi | Q2TZB2 |
SMRi | Q2TZB2 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 510516.Q2TZB2 |
Proteomic databases
PRIDEi | Q2TZB2 |
Organism-specific databases
VEuPathDBi | FungiDB:AO090011000926 |
Phylogenomic databases
OMAi | YHGNTNY |
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, 1 hit |
Pfami | View protein in Pfam PF13434, K_oxygenase, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | SIDA_ASPOR | |
Accessioni | Q2TZB2Primary (citable) accession number: Q2TZB2 Secondary accession number(s): Q8J2V1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 26, 2014 |
Last sequence update: | November 26, 2014 | |
Last modified: | May 25, 2022 | |
This is version 72 of the entry and version 2 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