NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=1021;
DOI=10.1078/0944-5013-00200; PubMed=14521231 [NCBI, ExPASy, EBI, Israel, Japan]
Lira-Ruan V., Sarath G., Klucas R.V., Arredondo-Peter R.;
"In silico analysis of a flavohemoglobin from Sinorhizobium meliloti strain 1021.";
Microbiol. Res. 158:215-227(2003).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1021;
DOI=10.1073/pnas.161294798; PubMed=11481432 [NCBI, ExPASy, EBI, Israel, Japan]
Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C., Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A., Long S.R.;
"Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid.";
Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).

Comments

FUNCTION: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress (By similarity).
CATALYTIC ACTIVITY: 2 NO + 2 O₂ + NAD(P)H = 2 NO₃^- + NAD(P)⁺.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit (By similarity).
COFACTOR: Binds 1 FAD per subunit (By similarity).
DOMAIN: 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.
SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins subfamily.
SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.

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

AY328026; AAP93662.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE006469; AAK65307.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A95343; A95343.

RefSeq

NP_435895.1; -.

3D structure databases

HSSP

P39662; 1CQX. [HSSP ENTRY / PDB]

SMR

Q7WUM8; 1-403.

ModBase

Q7WUM8.

Enzyme and pathway databases

BioCyc

SMEL266834:SMA1191-MON; -.

Ontologies

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.
IPR000778; GP91PhoX.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR001221; Phe_hydroxylase.
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.
PR00466; GP91PHOX.
PR00410; PHEHYDRXLASE.

PROSITE

PS51384; FAD_FR; 1.
PS01033; GLOBIN; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q7WUM8.

Genome annotation databases

1235685; -.

AE006469_GR; RA0649.

sme:SMa1191; -.

fig|266834.1.peg.649; -.

Phylogenomic databases

HOGENOM

Q7WUM8; -.

Genome annotation databases

CMR

Q7WUM8; RA0649.

Other

ProtoNet

Q7WUM8.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Detoxification; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP; Oxidoreductase; Oxygen transport; Plasmid; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 403`	`403`	`Flavohemoprotein.`	`PRO_0000052442`
`DOMAIN`	`152 262`	`111`	`FAD-binding FR-type.`
`NP_BIND`	`206 209`	`4`	`FAD (By similarity).`
`NP_BIND`	`275 280`	`6`	`NADP (By similarity).`
`NP_BIND`	`395 398`	`4`	`FAD (By similarity).`
`REGION`	`1 138`	`138`	`Globin.`
`REGION`	`149 403`	`255`	`Reductase.`
`REGION`	`266 403`	`138`	`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`	`394 394`	`1`	`Influences the redox potential of the prosthetic heme and FAD groups (By similarity).`
`CONFLICT`	`41 41`		`N -> D (in Ref. 1; AAP93662).`
`CONFLICT`	`88 88`		`L -> I (in Ref. 1; AAP93662).`
`CONFLICT`	`142 142`		`E -> G (in Ref. 1; AAP93662).`
`CONFLICT`	`250 250`		`L -> P (in Ref. 1; AAP93662).`
`CONFLICT`	`353 353`		`K -> N (in Ref. 1; AAP93662).`

Sequence information

Length: 403 AA [This is the length of the unprocessed precursor]

Molecular weight: 44775 Da [This is the MW of the unprocessed precursor]

CRC64: 935362921C3070CC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLTQKTKDIV KATAPVLAQH GYAIIQHFYK RMFQAHPELK NIFNMAHQER GEQQQALARA 

        70         80         90        100        110        120 
VYAYAANIEN PESLSAVLKD IAHKHASLGV RPEQYPIVGE HLLASIKEVL GDAATDEIIS 

       130        140        150        160        170        180 
AWAQAYGNLA DILAGMESEL YERSEERAGG WAGWRRFIVR EKNPESDVIT SFVLEPADGG 

       190        200        210        220        230        240 
PVADFEPGQY TSVAVQVPKL GYQQIRQYSL SDSPNGRSYR ISVKREDGGL GTPGYVSSLL 

       250        260        270        280        290        300 
HDEINVGDEL KLAAPYGNFY IDVSATTPIV LISGGVGLTP MVSMLKKALQ TPPRKVVFVH 

       310        320        330        340        350        360 
GARNSAVHAM RDRLKEASRT YPDFKLFIFY DEPLPTDIEG RDYDFAGLVD VEKVKDSILL 

       370        380        390        400 
DDADYYICGP VPFMRMQHDK LLGLGITEAR IHYEVFGPDL FAE

Q7WUM8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools