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UniProtKB/Swiss-Prot entry Q9RYR5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HMP_DEIRA
Primary accession number Q9RYR5
Secondary accession numbers None
Integrated into Swiss-Prot on September 13, 2004
Sequence was last modified on May 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 50)
Name and origin of the protein
Protein name Flavohemoprotein
Synonyms Hemoglobin-like protein
Flavohemoglobin
Nitric oxide dioxygenase
NO oxygenase
NOD
EC 1.14.12.17
Gene name
Name: hmp
OrderedLocusNames: DR_A0243
From
Deinococcus radiodurans [TaxID: 1299] [HAMAP proteome]
Taxonomy Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae; Deinococcus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1;
DOI=10.1126/science.286.5444.1571; PubMed=10567266 [NCBI, ExPASy, EBI, Israel, Japan]
White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.;
"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1.";
Science 286:1571-1577(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE001825; AAF12394.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D75577; D75577.
RefSeq NP_285566.1; -.
3D structure databases
HSSP P04252; 4VHB. [HSSP ENTRY / PDB]
ModBase Q9RYR5.
Enzyme and pathway databases
BioCyc DRAD243230:DR_A0243-MON; -.
Ontologies
GO
GO:0008941; Molecular function: nitric oxide dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0005344; Molecular function: oxygen transporter activity (inferred from electronic annotation from HAMAP).
GO:0015671; Biological process: oxygen transport (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01252; -; 1.
PBIL [Tree]
InterPro IPR001709; FPN_cyt_redctse.
IPR012292; Globin.
IPR000971; Globin_subset.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR000951; Ph_dOase_redase_FPNCR.
Graphical view of domain structure.
Gene3D G3DSA:1.10.490.10; Globin_related; 1.
Pfam PF00970; FAD_binding_6; 1.
PF00042; Globin; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00371; FPNCR.
PR00409; PHDIOXRDTASE.
PROSITE PS51384; FAD_FR; 1.
PS01033; GLOBIN; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9RYR5.
Genome annotation databases
GeneID 1798115; -.
GenomeReviews AE001825_GR; DR_A0243.
KEGG dra:DR_A0243; -.
NMPDR fig|243230.1.peg.3056; -.
TIGR DR_A0243; -.
Phylogenomic databases
HOGENOM Q9RYR5; -.
Other
ProtoNet Q9RYR5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP; Oxidoreductase; Oxygen transport; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   403  403     Flavohemoprotein. PRO_0000052430
DOMAIN   152   257  106     FAD-binding FR-type. 
NP_BIND   206   209  4     FAD (By similarity). 
NP_BIND   269   274  6     NADP (By similarity). 
NP_BIND   390   393  4     FAD (By similarity). 
REGION   1   138  138     Globin. 
REGION   149   403  255     Reductase. 
REGION   261   403  143     NAD or NADP-binding. 
ACT_SITE   95    95        Charge relay system (By similarity). 
ACT_SITE   137   137        Charge relay system (By similarity). 
METAL   85    85        Iron (heme proximal ligand) (By similarity). 
BINDING   190   190        FAD (By similarity). 
SITE   29    29  1     Involved in heme-bound ligand stabilization and O-O bond activation (By similarity). 
SITE   84    84  1     Influences the redox potential of the prosthetic heme and FAD groups (By similarity). 
SITE   389   389  1     Influences the redox potential of the prosthetic heme and FAD groups (By similarity). 
Sequence information
Length: 403 AA [This is the length of the unprocessed precursor] Molecular weight: 43296 Da [This is the MW of the unprocessed precursor] CRC64: 7402654E60039312 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLTPEQKAIV KATVPALEAH GETITRTFYA SMFAAHPELL NIFNPANQQT GKQARSLAAS 

        70         80         90        100        110        120 
VLAYAAHIDH PEALGGMVGR IAHKHVSLEV LPEHYPIVGQ YLLGAIAGVL GDAAKPEILD 

       130        140        150        160        170        180 
AWAAAYGELA DLMIGIEKGM YDAGAGQPGG WRDFRPFRVA RKVAESRVIT SFVLEPVGGG 

       190        200        210        220        230        240 
ALPAYQPGQY LSLKVKVPGQ ERWQIRQYSL SDAPSPDHYR ISVKREGGGL VSEYLHGAVQ 

       250        260        270        280        290        300 
EGDELLVHVP AGDFVLQQSE RPVVLISAGV GITPMLAMVQ TLAQAGSQRP VTFIHAAQNG 

       310        320        330        340        350        360 
SVHAFRDDVA RLTHEYPHFR KVVFYDEAGP DDQLGTHHDV AGRLSLDAVR GALPAGEAEF 

       370        380        390        400 
YYCGPAGFAG AVEAILDDLQ VPAERRFTET FGPSQSFAPV ILG
Q9RYR5 in FASTA format

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