Q7UIY1 (HMP_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Flavohemoprotein

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

Gene names

Name:	hmp
Synonyms:	fhp
Ordered Locus Names:	RB12262

Organism

Rhodopirellula baltica (strain SH1)

Taxonomic identifier

243090 [NCBI]

Taxonomic lineage

Bacteria › Planctomycetes › Planctomycetacia › Planctomycetales › Planctomycetaceae › Rhodopirellula

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

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. 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.
Sequence caution	The sequence CAD77481.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Oxygen transport Transport
Ligand	FAD Flavoprotein Heme Iron Metal-binding NAD NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	response to nitrosative stress Inferred from electronic annotation. Source: InterPro
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro nitric oxide dioxygenase activity Inferred from electronic annotation. Source: EC oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 408	408	Flavohemoprotein HAMAP MF_01252		PRO_0000052443
Regions
	Domain	152 – 263	112	FAD-binding FR-type
	Nucleotide binding	205 – 208	4	FAD By similarity
	Nucleotide binding	277 – 282	6	NADP By similarity
	Nucleotide binding	398 – 401	4	FAD By similarity
	Region	1 – 138	138	Globin HAMAP MF_01252
	Region	149 – 408	260	Reductase HAMAP MF_01252
	Region	267 – 408	142	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	397	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7UIY1 [UniParc]. Last modified September 13, 2004. Version 2. Checksum: B33B7EBC66316C1C	FASTA	408	44,911
	10 20 30 40 50 60 MLSEKTIRIV KEITPLVAAN AETITRRFYE RMFEANPEVK AFFNQAHQHS GGQQKALAGA 70 80 90 100 110 120 ICAYFTHIDN PAVLMPAVEL IAQKHVSLGI KPEHYPIVGS NLLAAIGDVM GDAATPEIVE 130 140 150 160 170 180 AVSEAYGFLA DIFIGREGAI YEEQASMPGG WNGTRTFVVT KKVRESEIVT SFYLKPEDEG 190 200 210 220 230 240 PLPPFKPGQY ITVHMDHPHT PTSPRNYSLS DCASQPHYRI SVKREERLVP DAPDGLISNH 250 260 270 280 290 300 LHDGIEEGHR IELGPPCGEF TVDPATIAKP IVLIAGGIGV TPLLSMAKSI VHANPNAELH 310 320 330 340 350 360 FIQAARNSKV HAFADELRRL AQAGPNVHTK VIYDSPLPGD VEEGKCDEAG FVTENQIRES 370 380 390 400 TPFTDADFYF CGPKPFMKNV HSCLRELGVD EHRVRYEFFG PKEELVAV

References

[1]

"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1." Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R. Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed: 12835416] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SH1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX294154 Genomic DNA. Translation: CAD77481.1. Different initiation.
RefSeq	NP_870404.1. NC_005027.1.
3D structure databases
ProteinModelPortal	Q7UIY1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1794152.
GenomeReviews	Gene locus RB12262 in contig BX119912_GR.
KEGG	rba:RB12262.
NMPDR	fig|243090.1.peg.6744.
PATRIC	23253383. VBIRhoBal59814_5920.
Phylogenomic databases
HOGENOM	HBG623097.
PhylomeDB	Q7UIY1.
ProtClustDB	PRK13289.
Enzyme and pathway databases
BioCyc	PSP117:RB12262-MONOMER.
Family and domain databases
HAMAP	MF_01252. Hmp. [Tree]
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR009050. Globin-like. IPR012292. Globin_dom. IPR000971. Globin_subset. IPR023950. Hmp. IPR001834. NADH-Cyt_B5_reductase. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD-bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Gene3D	G3DSA:1.10.490.10. Globin_related. 1 hit.
KO	K05916.
Pfam	PF00970. FAD_binding_6. 1 hit. PF00042. Globin. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view]
PRINTS	PR00406. CYTB5RDTASE.
SUPFAM	SSF46458. Globin_like. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HMP_RHOBA

Accession

Primary (citable) accession number: Q7UIY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	September 13, 2004
Last modified:	January 25, 2012
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program