Reviewed, UniProtKB/Swiss-Prot P39676 (FHP_YEAST)

Names and origin

Protein names

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

Gene names

Name:	YHB1
Synonyms:	YHB
Ordered Locus Names:	YGR234W
ORF Names:	G8572

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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 fungus from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. In the presence of oxygen and NADH, it has NADH oxidase activity, which leads to the generation of superoxide and H(2)O(2). Under anaerobic conditions, it also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity.
Catalytic activity	2 NO + 2 O(2) + NAD(P)H = 2 NO(3)(-) + NAD(P)(+).
Cofactor	Binds 1 FAD per subunit. Binds 1 heme B group per subunit.
Subcellular location	CytoplasmBy similarity.
Domain	Consists of two distinct domains; a N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
Miscellaneous	Present with 13000 molecules/cell in log phase SD medium.
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
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein Heme Iron Metal-binding NAD NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW oxygen transport Inferred from electronic annotation. Source: InterPro response to stress Ref.7 Ref.8 Inferred from direct assay. Source: SGD response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: SGD mitochondrial matrix Inferred from direct assay. Source: SGD
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: EC nitric oxide reductase activity Ref.10 Inferred from mutant phenotype. Source: SGD oxygen binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 399	399	Flavohemoprotein		PRO_0000052458
Regions
	Domain	147 – 264	118	FAD-binding FR-type
	Nucleotide binding	207 – 210	4	FAD By similarity
	Nucleotide binding	281 – 286	6	NADP By similarity
	Nucleotide binding	389 – 392	4	FAD By similarity
	Region	1 – 138	138	Globin
	Region	146 – 399	254	Reductase
	Region	272 – 399	128	NAD or NADP-binding
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	189	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
Amino acid modifications
	Modified residue	22	1	Phosphothreonine
	Modified residue	210	1	Phosphoserine
Natural variations
	Natural variant	153	1	D → E in strain: JM43.
	Natural variant	345	1	N → D in strain: JM43.
	Natural variant	365	1	L → V in strain: JM43.

Sequences

	Sequence		Length	Mass (Da)
	P39676-1 [UniParc]. Last modified February 21, 2006. Version 2. Checksum: 8AF1DE3280220D56	FASTA	399	44,646
	10 20 30 40 50 60 MLAEKTRSII KATVPVLEQQ GTVITRTFYK NMLTEHTELL NIFNRTNQKV GAQPNALATT 70 80 90 100 110 120 VLAAAKNIDD LSVLMDHVKQ IGHKHRALQI KPEHYPIVGE YLLKAIKEVL GDAATPEIIN 130 140 150 160 170 180 AWGEAYQAIA DIFITVEKKM YEEALWPGWK PFDITAKEYV ASDIVEFTVK PKFGSGIELE 190 200 210 220 230 240 SLPITPGQYI TVNTHPIRQE NQYDALRHYS LCSASTKNGL RFAVKMEAAR ENFPAGLVSE 250 260 270 280 290 300 YLHKDAKVGD EIKLSAPAGD FAINKELIHQ NEVPLVLLSS GVGVTPLLAM LEEQVKCNPN 310 320 330 340 350 360 RPIYWIQSSY DEKTQAFKKH VDELLAECAN VDKIIVHTDT EPLINAAFLK EKSPAHADVY 370 380 390 TCGSLAFMQA MIGHLKELEH RDDMIHYEPF GPKMSTVQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Yeast flavohemoglobin is an ancient protein related to globins and a reductase family." Zhu H., Riggs A.F. Proc. Natl. Acad. Sci. U.S.A. 89:5015-5019(1992) [PubMed: 1594608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 1-31, VARIANTS GLU-153; ASP-345 AND VAL-365. Strain: DBY939 and JM43.
[2]	"Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1 region from the right arm of Saccharomyces cerevisiae chromosome VII." van der Aart Q.J.M., Kleine K., Steensma H.Y. Yeast 12:385-390(1996) [PubMed: 8701610] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	Perez-Ortin J.E. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36. Strain: T73.
[6]	"Regulation of Saccharomyces cerevisiae flavohemoglobin gene expression." Crawford M.J., Sherman D.R., Goldberg D.E. J. Biol. Chem. 270:6991-6996(1995) [PubMed: 7896850] [Abstract] Cited for: REGULATION OF EXPRESSION.
[7]	"Function and expression of flavohemoglobin in Saccharomyces cerevisiae. Evidence for a role in the oxidative stress response." Buisson N., Labbe-Bois R. J. Biol. Chem. 271:25131-25138(1996) [PubMed: 8810268] [Abstract] Cited for: ROLE IN OXIDATIVE STRESS.
[8]	"Flavohemoglobin expression and function in Saccharomyces cerevisiae. No relationship with respiration and complex response to oxidative stress." Buisson N., Labbe-Bois R. J. Biol. Chem. 273:9527-9533(1998) [PubMed: 9545281] [Abstract] Cited for: ROLE IN OXIDATIVE STRESS.
[9]	"Nitric-oxide dioxygenase activity and function of flavohemoglobins. Sensitivity to nitric oxide and carbon monoxide inhibition." Gardner P.R., Gardner A.M., Martin L.A., Dou Y., Li T., Olson J.S., Zhu H., Riggs A.F. J. Biol. Chem. 275:31581-31587(2000) [PubMed: 10922365] [Abstract] Cited for: ENZYME ACTIVITY.
[10]	"Protection from nitrosative stress by yeast flavohemoglobin." Liu L., Zeng M., Hausladen A., Heitman J., Stamler J.S. Proc. Natl. Acad. Sci. U.S.A. 97:4672-4676(2000) [PubMed: 10758168] [Abstract] Cited for: ROLE IN NITRIC OXIDE DETOXIFICATION.
[11]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22 AND SER-210, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L07070 mRNA. No translation available. L07071 Genomic DNA. No translation available. X87941 Genomic DNA. Translation: CAA61184.1. Z73019 Genomic DNA. Translation: CAA97262.1. AY692964 Genomic DNA. Translation: AAT92983.1. AF239759 Genomic DNA. Translation: AAK15081.1.
PIR	S57699.
RefSeq	NP_011750.1.
3D structure databases
HSSP	HSSP built from PDB template 1VHB based on UniProtKB P04252.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1355N.
IntAct	P39676.
Proteomic databases
PeptideAtlas	P39676.
Genome annotation databases
Ensembl	YGR234W. Saccharomyces cerevisiae. [Contig view]
GeneID	853149.
GenomeReviews	Gene locus YGR234W in contig Y13135_GR.
KEGG	sce:YGR234W.
NMPDR	fig|4932.3.peg.2878.
Organism-specific databases
CYGD	YGR234w.
SGD	S000003466. YHB1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P39676.
Gene expression databases
ArrayExpress	P39676.
GermOnline	YGR234W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR012292. Globin. IPR000971. Globin_subset. IPR008333. OxRdtase_FAD-bd. IPR001433. OxRdtase_FAD/NAD_bd. [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]
PROSITE	PS51384. FAD_FR. 1 hit. PS01033. GLOBIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
LinkHub	P39676.
NextBio	973231.

Entry information

Entry name

FHP_YEAST

Accession

Primary (citable) accession number: P39676
Secondary accession number(s): Q6B1W6, Q9C1R6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 21, 2006
Last modified:	November 25, 2008
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)