Reviewed, UniProtKB/Swiss-Prot Q87F90 (HMP_XYLFT)

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:	hmpA
Ordered Locus Names:	PD_0038

Organism

Xylella fastidiosa (strain Temecula1 / ATCC 700964) [Complete proteome] [HAMAP]

Taxonomic identifier

183190 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xylella

Protein attributes

Sequence length	397 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
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	electron carrier activity Inferred from electronic annotation. Source: InterPro 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 – 397	397	Flavohemoprotein HAMAP MF_01252		PRO_0000052454
Regions
	Domain	154 – 258	105	FAD-binding FR-type
	Nucleotide binding	207 – 210	4	FAD By similarity
	Nucleotide binding	271 – 276	6	NADP By similarity
	Nucleotide binding	387 – 390	4	FAD By similarity
	Region	1 – 140	140	Globin HAMAP MF_01252
	Region	151 – 397	247	Reductase HAMAP MF_01252
	Region	261 – 397	137	NAD or NADP-binding HAMAP MF_01252
Sites
	Active site	97	1	Charge relay system By similarity
	Active site	139	1	Charge relay system By similarity
	Metal binding	87	1	Iron (heme proximal ligand) By similarity
	Binding site	192	1	FAD By similarity
	Site	32	1	Involved in heme-bound ligand stabilization and O-O bond activation By similarity
	Site	86	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity
	Site	386	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q87F90-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 7C68FF4A44AC8EEC	FASTA	397	44,089
	10 20 30 40 50 60 MSASFSPHTI TLIKSTVPLL AEHGTTIIEA MYHRLFEDPQ IEALFNQANQ KNGTQIHALA 70 80 90 100 110 120 GAILAYARNI DNPGVLASAI ERISQKHVGY AIHPEHYPHV ATALLGAIKQ VLGDVATSEV 130 140 150 160 170 180 LEAWGEAYWF IANLLKDREA VIREGIMTKN GGWIHWRRFV ISKRIPESET ITSFMLHPED 190 200 210 220 230 240 GGPVVPHQAG QYLTFRFDAA GMPGMKRNYS ISCGPNSDHY RITVKREHGT GASAFLHDQA 250 260 270 280 290 300 KVGTIIECTP PVGDFFLPSV IERPIVLLSG GVGLTPMVSM MEQIAEAYPD AQVWYVHGTQ 310 320 330 340 350 360 NRETHAMDAH IRALVSRHKH MKATTFYTQR SEADDAEAGF ITIDWLRANT PFQKADFYLC 370 380 390 GPRPFLRTFV RDLIGAGVPA AQVHYEFFGP MDEEMAA

References

[1]

"Comparative analyses of the complete genome sequences of Pierce's disease and citrus variegated chlorosis strains of Xylella fastidiosa." Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M. , Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P. J. Bacteriol. 185:1018-1026(2003) [PubMed: 12533478] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009442 Genomic DNA. Translation: AAO27945.1.
RefSeq	NP_778296.1.
3D structure databases
SMR	Q87F90. Positions 5-391.
ModBase	Search...
Protein-protein interaction databases
STRING	Q87F90.
Genome annotation databases
GeneID	1144238.
GenomeReviews	Gene locus PD_0038 in contig AE009442_GR.
KEGG	xft:PD0038.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1018.
HOGENOM	HBG623097.
OMA	KQIGHKH.
Enzyme and pathway databases
BioCyc	XFAS183190:PD_0038-MONOMER.
Family and domain databases
HAMAP	MF_01252. Hmp. [Tree]
InterPro	IPR017927. Fd_Rdtase_FAD-bd. IPR012292. Globin. IPR009050. Globin-like. IPR000971. Globin_subset. IPR008333. OxRdtase_FAD-bd_dom. IPR001433. OxRdtase_FAD/NAD_bd. IPR000951. Ph_dOase_redase_FPNCR. 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	PR00409. PHDIOXRDTASE.
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HMP_XYLFT

Accession

Primary (citable) accession number: Q87F90

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	June 1, 2003
Last modified:	January 19, 2010
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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