Reviewed, UniProtKB/Swiss-Prot Q7WUM8 (HMP_RHIME)

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

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O2 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. HAMAP MF_01252
Catalytic activity	2 NO + 2 O2 + NAD(P)H = 2 NO3- + NAD(P)+. HAMAP MF_01252
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity. HAMAP MF_01252 Binds 1 FAD per subunit By similarity. HAMAP MF_01252
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. HAMAP MF_01252
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.

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
Molecular function	heme 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 403	403	Flavohemoprotein HAMAP MF_01252		PRO_0000052442
Regions
	Domain	152 – 262	111	FAD-binding FR-type
	Nucleotide binding	206 – 209	4	FAD By similarity
	Nucleotide binding	275 – 280	6	NADP By similarity
	Nucleotide binding	395 – 398	4	FAD By similarity
	Region	1 – 138	138	Globin HAMAP MF_01252
	Region	149 – 403	255	Reductase HAMAP MF_01252
	Region	266 – 403	138	NAD or NADP-binding HAMAP MF_01252
Sites
	Active site	95	1	Charge relay system By similarity
	Active site	137	1	Charge relay system By similarity
	Metal binding	85	1	Iron (heme proximal ligand) By similarity
	Binding site	190	1	FAD By similarity
	Site	29	1	Involved in heme-bound ligand stabilization and O-O bond activation By similarity
	Site	84	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity
	Site	394	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity
Experimental info
	Sequence conflict	41	1	N → D in AAP93662. Ref.1
	Sequence conflict	88	1	L → I in AAP93662. Ref.1
	Sequence conflict	142	1	E → G in AAP93662. Ref.1
	Sequence conflict	250	1	L → P in AAP93662. Ref.1
	Sequence conflict	353	1	K → N in AAP93662. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q7WUM8-1 [UniParc]. Last modified September 13, 2004. Version 2. Checksum: 935362921C3070CC	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

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. , Palm C., Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A., 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY328026 Genomic DNA. Translation: AAP93662.1. AE006469 Genomic DNA. Translation: AAK65307.1.
PIR	A95343.
RefSeq	NP_435895.1.
3D structure databases
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	HBG623097.
OMA	YSISCAP.
Enzyme and pathway databases
BioCyc	SMEL266834:SMA1191-MONOMER.
BRENDA	1.14.12.17. 142.
Family and domain databases
HAMAP	MF_01252. Hmp. [Tree]
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR012292. Globin. IPR009050. Globin-like. IPR000971. Globin_subset. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD_bd. IPR001221. Phe_hydroxylase. IPR017938. Riboflavin_synthase-like_b-brl. [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. PR00410. PHEHYDRXLASE.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

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:	January 19, 2010
This is version 50 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)