Flavohemoprotein - Rhizobium meliloti

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Reviewed, UniProtKB/Swiss-Prot Q7WUM8 (HMP_RHIME)

Last modified November 25, 2008. Version 40. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Flavohemoprotein
Alternative name(s):
    Hemoglobin-like protein
    Flavohemoglobin
    Nitric oxide dioxygenase
      Short name=NO oxygenase
      Short name=NOD
    EC=1.14.12.17

Gene names

Name:	hmp
Synonyms:	fhb
Ordered Locus Names:	RA0649
ORF Names:	SMa1191

Encoded on

Plasmid pSymA (megaplasmid 1)

Organism

Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

382 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

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Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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General annotation (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 O(2) + NAD(P)H = 2 NO(3)(-) + NAD(P)(+).
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. 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.
Sequence similarities	Belongs to the globin family. Two-domain flavohemoproteins subfamily. In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. Contains 1 FAD-binding FR-type domain.

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Ontologies

Keywords
Biological process	Detoxification Oxygen transport Transport
Ligand	FAD Flavoprotein Heme Iron Metal-binding NAD NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Plasmid
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen transport Inferred from electronic annotation. Source: HAMAP response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Inferred from electronic annotation. Source: InterPro
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro nitric oxide dioxygenase activity Inferred from electronic annotation. Source: HAMAP oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 403

403

Flavohemoprotein

PRO_0000052442

Regions

Domain

152 – 262

111

FAD-binding FR-type

Nucleotide binding

206 – 209

FAD By similarity

Nucleotide binding

275 – 280

NADP By similarity

Nucleotide binding

395 – 398

FAD By similarity

Region

1 – 138

138

Globin

Region

149 – 403

255

Reductase

Region

266 – 403

138

NAD or NADP-binding

Sites

Active site

Charge relay system By similarity

Active site

137

Charge relay system By similarity

Metal binding

Iron (heme proximal ligand) By similarity

Binding site

190

FAD By similarity

Site

Involved in heme-bound ligand stabilization and O-O bond activation By similarity

Site

Influences the redox potential of the prosthetic heme and FAD groups By similarity

Site

394

Influences the redox potential of the prosthetic heme and FAD groups By similarity

Experimental info

Sequence conflict

N → D in AAP93662. Ref.1

Sequence conflict

L → I in AAP93662. Ref.1

Sequence conflict

142

E → G in AAP93662. Ref.1

Sequence conflict

250

L → P in AAP93662. Ref.1

Sequence conflict

353

K → N in AAP93662. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q7WUM8-1 [UniParc].

Last modified September 13, 2004. Version 2.
Checksum: 935362921C3070CC
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FASTA

403

44,775

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"In silico analysis of a flavohemoglobin from Sinorhizobium meliloti strain 1021." Lira-Ruan V., Sarath G., Klucas R.V., Arredondo-Peter R. Microbiol. Res. 158:215-227(2003) [PubMed: 14521231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 1021.
[2]	"Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid." 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. Long S.R. Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001) [PubMed: 11481432] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

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Cross-references

Sequence databases
	AY328026 Genomic DNA. Translation: AAP93662.1. AE006469 Genomic DNA. Translation: AAK65307.1.
PIR	A95343.
RefSeq	NP_435895.1.
3D structure databases
HSSP	HSSP built from PDB template 1CQX based on UniProtKB P39662.
SMR	Q7WUM8. Positions 1-403.
ModBase	Search...
Genome annotation databases
GeneID	1235685.
GenomeReviews	Gene locus RA0649 in contig AE006469_GR.
KEGG	sme:SMa1191.
NMPDR	fig\|266834.1.peg.649.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7WUM8.
Enzyme and pathway databases
BioCyc	SMEL266834:SMA1191-MON.
Family and domain databases
HAMAP	MF_01252. [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]
Gene3D	G3DSA:1.10.490.10. Globin_related. 1 hit.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00042. Globin. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00371. FPNCR. PR00466. GP91PHOX. PR00410. PHEHYDRXLASE.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

HMP_RHIME

Accession

Primary (citable) accession number: Q7WUM8
Secondary accession number(s): Q92Z48

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	September 13, 2004
Last modified:	November 25, 2008
This is version 40 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents