UniProtKB - Q9RYR5 (HMP_DEIRA)
Protein
Flavohemoprotein
Gene
hmp
Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Functioni
Catalytic activityi
- EC:1.14.12.17UniRule annotation
- EC:1.14.12.17UniRule annotation
Cofactori
Protein has several cofactor binding sites:- heme bUniRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.UniRule annotation
- FADUniRule annotationNote: Binds 1 FAD per subunit.UniRule annotation
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 29 | Involved in heme-bound ligand stabilization and O-O bond activationUniRule annotation | 1 | |
Sitei | 84 | Influences the redox potential of the prosthetic heme and FAD groupsUniRule annotation | 1 | |
Metal bindingi | 85 | Iron (heme proximal ligand)UniRule annotation | 1 | |
Active sitei | 95 | Charge relay systemUniRule annotation | 1 | |
Active sitei | 137 | Charge relay systemUniRule annotation | 1 | |
Binding sitei | 190 | FADUniRule annotation | 1 | |
Sitei | 389 | Influences the redox potential of the prosthetic heme and FAD groupsUniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 206 – 209 | FADUniRule annotation | 4 | |
Nucleotide bindingi | 269 – 274 | NADPUniRule annotation | 6 | |
Nucleotide bindingi | 390 – 393 | FADUniRule annotation | 4 |
GO - Molecular functioni
- FAD binding Source: GO_Central
- heme binding Source: InterPro
- metal ion binding Source: UniProtKB-KW
- nitric oxide dioxygenase activity Source: GO_Central
- oxygen binding Source: InterPro
- oxygen carrier activity Source: UniProtKB-UniRule
GO - Biological processi
- cellular response to nitrosative stress Source: GO_Central
- nitric oxide catabolic process Source: GO_Central
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Oxygen transport, Transport |
Ligand | FAD, Flavoprotein, Heme, Iron, Metal-binding, NAD, NADP |
Names & Taxonomyi
Protein namesi | Recommended name: FlavohemoproteinUniRule annotationAlternative name(s): FlavohemoglobinUniRule annotation Hemoglobin-like proteinUniRule annotation Nitric oxide dioxygenaseUniRule annotation (EC:1.14.12.17UniRule annotation) Short name: NO oxygenaseUniRule annotation Short name: NODUniRule annotation |
Gene namesi | Name:hmpUniRule annotation Ordered Locus Names:DR_A0243 |
Organismi | Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) |
Taxonomic identifieri | 243230 [NCBI] |
Taxonomic lineagei | Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000052430 | 1 – 403 | FlavohemoproteinAdd BLAST | 403 |
Structurei
3D structure databases
ProteinModelPortali | Q9RYR5 |
SMRi | Q9RYR5 |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 152 – 257 | FAD-binding FR-typeUniRule annotationAdd BLAST | 106 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 138 | GlobinAdd BLAST | 138 | |
Regioni | 149 – 403 | ReductaseAdd BLAST | 255 | |
Regioni | 261 – 403 | NAD or NADP-bindingAdd BLAST | 143 |
Domaini
Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
Sequence similaritiesi
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.UniRule annotation
Phylogenomic databases
eggNOGi | ENOG4105CJJ Bacteria COG1017 LUCA COG1018 LUCA |
HOGENOMi | HOG000238921 |
InParanoidi | Q9RYR5 |
KOi | K05916 |
OMAi | MFAHNPE |
OrthoDBi | 1834577at2 |
Family and domain databases
Gene3Di | 1.10.490.10, 1 hit 3.40.50.80, 1 hit |
HAMAPi | MF_01252 Hmp, 1 hit |
InterProi | View protein in InterPro IPR008333 Cbr1-like_FAD-bd_dom IPR017927 FAD-bd_FR_type IPR001709 Flavoprot_Pyr_Nucl_cyt_Rdtase IPR039261 FNR_nucleotide-bd IPR000971 Globin IPR009050 Globin-like_sf IPR012292 Globin/Proto IPR023950 Hmp IPR001433 OxRdtase_FAD/NAD-bd IPR000951 Ph_dOase_redase IPR017938 Riboflavin_synthase-like_b-brl |
PANTHERi | PTHR43396 PTHR43396, 1 hit |
Pfami | View protein in Pfam PF00970 FAD_binding_6, 1 hit PF00042 Globin, 1 hit PF00175 NAD_binding_1, 1 hit |
PRINTSi | PR00371 FPNCR PR00409 PHDIOXRDTASE |
SUPFAMi | SSF46458 SSF46458, 1 hit SSF52343 SSF52343, 1 hit SSF63380 SSF63380, 1 hit |
PROSITEi | View protein in PROSITE PS51384 FAD_FR, 1 hit PS01033 GLOBIN, 1 hit |
i Sequence
Sequence statusi: Complete.
Q9RYR5-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLTPEQKAIV KATVPALEAH GETITRTFYA SMFAAHPELL NIFNPANQQT
60 70 80 90 100
GKQARSLAAS VLAYAAHIDH PEALGGMVGR IAHKHVSLEV LPEHYPIVGQ
110 120 130 140 150
YLLGAIAGVL GDAAKPEILD AWAAAYGELA DLMIGIEKGM YDAGAGQPGG
160 170 180 190 200
WRDFRPFRVA RKVAESRVIT SFVLEPVGGG ALPAYQPGQY LSLKVKVPGQ
210 220 230 240 250
ERWQIRQYSL SDAPSPDHYR ISVKREGGGL VSEYLHGAVQ EGDELLVHVP
260 270 280 290 300
AGDFVLQQSE RPVVLISAGV GITPMLAMVQ TLAQAGSQRP VTFIHAAQNG
310 320 330 340 350
SVHAFRDDVA RLTHEYPHFR KVVFYDEAGP DDQLGTHHDV AGRLSLDAVR
360 370 380 390 400
GALPAGEAEF YYCGPAGFAG AVEAILDDLQ VPAERRFTET FGPSQSFAPV
ILG
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE001825 Genomic DNA Translation: AAF12394.1 |
PIRi | D75577 |
RefSeqi | NP_285566.1, NC_001264.1 WP_010889502.1, NZ_CP015082.1 |
Genome annotation databases
EnsemblBacteriai | AAF12394; AAF12394; DR_A0243 |
GeneIDi | 1798115 |
KEGGi | dra:DR_A0243 |
PATRICi | fig|243230.17.peg.3133 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE001825 Genomic DNA Translation: AAF12394.1 |
PIRi | D75577 |
RefSeqi | NP_285566.1, NC_001264.1 WP_010889502.1, NZ_CP015082.1 |
3D structure databases
ProteinModelPortali | Q9RYR5 |
SMRi | Q9RYR5 |
ModBasei | Search... |
MobiDBi | Search... |
Protein-protein interaction databases
STRINGi | 243230.DR_A0243 |
Protocols and materials databases
Structural Biology Knowledgebase | Search... |
Genome annotation databases
EnsemblBacteriai | AAF12394; AAF12394; DR_A0243 |
GeneIDi | 1798115 |
KEGGi | dra:DR_A0243 |
PATRICi | fig|243230.17.peg.3133 |
Phylogenomic databases
eggNOGi | ENOG4105CJJ Bacteria COG1017 LUCA COG1018 LUCA |
HOGENOMi | HOG000238921 |
InParanoidi | Q9RYR5 |
KOi | K05916 |
OMAi | MFAHNPE |
OrthoDBi | 1834577at2 |
Family and domain databases
Gene3Di | 1.10.490.10, 1 hit 3.40.50.80, 1 hit |
HAMAPi | MF_01252 Hmp, 1 hit |
InterProi | View protein in InterPro IPR008333 Cbr1-like_FAD-bd_dom IPR017927 FAD-bd_FR_type IPR001709 Flavoprot_Pyr_Nucl_cyt_Rdtase IPR039261 FNR_nucleotide-bd IPR000971 Globin IPR009050 Globin-like_sf IPR012292 Globin/Proto IPR023950 Hmp IPR001433 OxRdtase_FAD/NAD-bd IPR000951 Ph_dOase_redase IPR017938 Riboflavin_synthase-like_b-brl |
PANTHERi | PTHR43396 PTHR43396, 1 hit |
Pfami | View protein in Pfam PF00970 FAD_binding_6, 1 hit PF00042 Globin, 1 hit PF00175 NAD_binding_1, 1 hit |
PRINTSi | PR00371 FPNCR PR00409 PHDIOXRDTASE |
SUPFAMi | SSF46458 SSF46458, 1 hit SSF52343 SSF52343, 1 hit SSF63380 SSF63380, 1 hit |
PROSITEi | View protein in PROSITE PS51384 FAD_FR, 1 hit PS01033 GLOBIN, 1 hit |
ProtoNeti | Search... |
Entry informationi
Entry namei | HMP_DEIRA | |
Accessioni | Q9RYR5Primary (citable) accession number: Q9RYR5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 13, 2004 |
Last sequence update: | May 1, 2000 | |
Last modified: | January 16, 2019 | |
This is version 114 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families