Reviewed, UniProtKB/Swiss-Prot Q8ZCR0 (HMP_YERPE)

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:	fsrB, hmp2, hmpA, hmpX
Ordered Locus Names:	YPO2908, y1321, YP_2547

Organism

Yersinia pestis [Complete proteome] [HAMAP]

Taxonomic identifier

632 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length	396 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	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 – 396	396	Flavohemoprotein HAMAP MF_01252		PRO_0000052455
Regions
	Domain	150 – 255	106	FAD-binding FR-type
	Nucleotide binding	204 – 207	4	FAD By similarity
	Nucleotide binding	268 – 273	6	NADP By similarity
	Nucleotide binding	389 – 392	4	FAD By similarity
	Region	1 – 136	136	Globin HAMAP MF_01252
	Region	147 – 396	250	Reductase HAMAP MF_01252
	Region	259 – 396	138	NAD or NADP-binding HAMAP MF_01252
Sites
	Active site	95	1	Charge relay system By similarity
	Active site	135	1	Charge relay system By similarity
	Metal binding	85	1	Iron (heme proximal ligand) By similarity
	Binding site	188	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	388	1	Influences the redox potential of the prosthetic heme and FAD groups By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8ZCR0-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 3280D7289C461B0B	FASTA	396	44,816
	10 20 30 40 50 60 MLDTQTIAIV KSTIPLLAAT GPKLTAHFYE RMFKHHPELK NIFNMSNQSS GDQREALFNA 70 80 90 100 110 120 ICAYATNIEN LAALLPTVER IAQKHTSLNI QPEHYPIVGE HLIATLDELF SPGQAVLDAW 130 140 150 160 170 180 AKAYGVLADV FIQRESQIYQ QSETETGGWR TLRRFRIIKK EQQSEVICSF VLAPEDGGQV 190 200 210 220 230 240 LHYKPGQYLG IYIEHESLEF QEIRQYSLTT APNGKTYRIA VKREEQGTVS NLLHRELNEG 250 260 270 280 290 300 DIVRIAPPRG DFFLDVSPDT PVALISAGVG QTPMLSMLNT LYSQQHAAPV HWLHAAENGR 310 320 330 340 350 360 VHAFADEVSA IAAKMPNLSR HVWYREPDLQ DKHGEDYHSQ GLMDLSSYQW LADDPKRHYY 370 380 390 FCGPLPFMQF IGRQLLAQGI APEQIHYECF GPHKVI

References

[1]	"Genome sequence of Yersinia pestis, the causative agent of plague." Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G. Nature 413:523-527(2001) [PubMed: 11586360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CO-92 / Biovar Orientalis.
[2]	"Genome sequence of Yersinia pestis KIM." Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. , Matson J.S., Blattner F.R., Perry R.D. J. Bacteriol. 184:4601-4611(2002) [PubMed: 12142430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KIM5 / Biovar Mediaevalis.
[3]	"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans." Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R. DNA Res. 11:179-197(2004) [PubMed: 15368893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL590842 Genomic DNA. Translation: CAL21519.1. AE009952 Genomic DNA. Translation: AAM84894.1. AE017042 Genomic DNA. Translation: AAS62743.1.
PIR	AD0354.
RefSeq	NP_668643.1. NP_993866.1. YP_002347842.1.
3D structure databases
SMR	Q8ZCR0. Positions 1-396.
ModBase	Search...
Genome annotation databases
GeneID	1146268. 1175732. 2766713.
GenomeReviews	Gene locus y1321 in contig AE009952_GR. Gene locus YP_2547 in contig AE017042_GR. Gene locus YPO2908 in contig AL590842_GR.
KEGG	ype:YPO2908. ypk:y1321. ypm:YP_2547.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG623097.
OMA	KQIGHKH.
Enzyme and pathway databases
BioCyc	YPES187410:Y1321-MONOMER. YPES214092:YPO2908-MONOMER. YPES229193:YP2547-MONOMER.
BRENDA	1.14.12.17. 142588.
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_YERPE

Accession

Primary (citable) accession number: Q8ZCR0
Secondary accession number(s): Q0WCZ6, Q74SP6, Q7CJP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	March 1, 2002
Last modified:	January 19, 2010
This is version 57 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)