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UniProtKB/Swiss-Prot entry P39676


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FHP_YEAST
Primary accession number P39676
Secondary accession numbers Q6B1W6 Q9C1R6
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 21, 2006 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 84)
Name and origin of the protein
Protein name Flavohemoprotein
Synonyms EC 1.14.12.17
Flavohemoglobin
Hemoglobin-like protein
Nitric oxide dioxygenase
NO oxygenase
NOD
Gene name
Name: YHB1
Synonyms: YHB
OrderedLocusNames: YGR234W
ORFNames: G8572
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 1-31, AND VARIANTS GLU-153; ASP-345 AND VAL-365.
STRAIN=DBY939, and JM43;
PubMed=1594608 [NCBI, ExPASy, EBI, Israel, Japan]
Zhu H., Riggs A.F.;
"Yeast flavohemoglobin is an ancient protein related to globins and a reductase family.";
Proc. Natl. Acad. Sci. U.S.A. 89:5015-5019(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/(SICI)1097-0061(19960330)12:4<385::AID-YEA910>3.3.CO;2-7; PubMed=8701610 [NCBI, ExPASy, EBI, Israel, Japan]
van der Aart Q.J.M., Kleine K., Steensma H.Y.;
"Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1 region from the right arm of Saccharomyces cerevisiae chromosome VII.";
Yeast 12:385-390(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
STRAIN=T73;
Perez-Ortin J.E.;
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[6]
REGULATION OF EXPRESSION.
DOI=10.1074/jbc.270.12.6991; PubMed=7896850 [NCBI, ExPASy, EBI, Israel, Japan]
Crawford M.J., Sherman D.R., Goldberg D.E.;
"Regulation of Saccharomyces cerevisiae flavohemoglobin gene expression.";
J. Biol. Chem. 270:6991-6996(1995).
[7]
ROLE IN OXIDATIVE STRESS.
DOI=10.1074/jbc.271.41.25699; PubMed=8810268 [NCBI, ExPASy, EBI, Israel, Japan]
Buisson N., Labbe-Bois R.;
"Function and expression of flavohemoglobin in Saccharomyces cerevisiae. Evidence for a role in the oxidative stress response.";
J. Biol. Chem. 271:25131-25138(1996).
[8]
ROLE IN OXIDATIVE STRESS.
DOI=10.1074/jbc.273.16.9527; PubMed=9545281 [NCBI, ExPASy, EBI, Israel, Japan]
Buisson N., Labbe-Bois R.;
"Flavohemoglobin expression and function in Saccharomyces cerevisiae. No relationship with respiration and complex response to oxidative stress.";
J. Biol. Chem. 273:9527-9533(1998).
[9]
ENZYME ACTIVITY.
DOI=10.1074/jbc.M004141200; PubMed=10922365 [NCBI, ExPASy, EBI, Israel, Japan]
Gardner P.R., Gardner A.M., Martin L.A., Dou Y., Li T., Olson J.S., Zhu H., Riggs A.F.;
"Nitric-oxide dioxygenase activity and function of flavohemoglobins. Sensitivity to nitric oxide and carbon monoxide inhibition.";
J. Biol. Chem. 275:31581-31587(2000).
[10]
ROLE IN NITRIC OXIDE DETOXIFICATION.
DOI=10.1073/pnas.090083597; PubMed=10758168 [NCBI, ExPASy, EBI, Israel, Japan]
Liu L., Zeng M., Hausladen A., Heitman J., Stamler J.S.;
"Protection from nitrosative stress by yeast flavohemoglobin.";
Proc. Natl. Acad. Sci. U.S.A. 97:4672-4676(2000).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22 AND SER-210, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 0:0-0(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L07070; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
L07071; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X87941; CAA61184.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73019; CAA97262.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY692964; AAT92983.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF239759; AAK15081.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S57699; S57699.
RefSeq NP_011750.1; -.
3D structure databases
HSSP P04252; 1VHB. [HSSP ENTRY / PDB]
ModBase P39676.
Protein-protein interaction databases
DIP DIP:1355N; -.
IntAct P39676; -.
Organism-specific databases
CYGD YGR234w; -.
SGD S000003466; YHB1.
Yeast-GFP YGR234W.
Gene expression databases
ArrayExpress P39676; -.
GermOnline YGR234W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from SGD).
GO:0005759; Cellular component: mitochondrial matrix (inferred from direct assay from SGD).
GO:0016966; Molecular function: nitric oxide reductase activity (inferred from mutant phenotype from SGD).
GO:0006950; Biological process: response to stress (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR012292; Globin.
IPR000971; Globin_subset.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:1.10.490.10; Globin_related; 1.
Pfam PF00970; FAD_binding_6; 1.
PF00042; Globin; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.
PROSITE PS51384; FAD_FR; 1.
PS01033; GLOBIN; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P39676.
Proteomic databases
PeptideAtlas P39676; -.
Genome annotation databases
Ensembl YGR234W; Saccharomyces cerevisiae. [Contig view]
GeneID 853149; -.
GenomeReviews Y13135_GR; YGR234W.
KEGG sce:YGR234W; -.
NMPDR fig|4932.3.peg.2878; -.
Phylogenomic databases
HOGENOM P39676; -.
Other
LinkHub P39676; -.
ProtoNet P39676.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Detoxification; Direct protein sequencing; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   399  399     Flavohemoprotein. PRO_0000052458
DOMAIN   147   264  118     FAD-binding FR-type. 
NP_BIND   207   210  4     FAD (By similarity). 
NP_BIND   281   286  6     NADP (By similarity). 
NP_BIND   389   392  4     FAD (By similarity). 
REGION   1   138  138     Globin. 
REGION   146   399  254     Reductase. 
REGION   272   399  128     NAD or NADP-binding. 
ACT_SITE   95    95        Charge relay system (By similarity). 
ACT_SITE   137   137        Charge relay system (By similarity). 
METAL   85    85        Iron (heme proximal ligand) (By similarity). 
BINDING   189   189        FAD (By similarity). 
SITE   29    29  1     Involved in heme-bound ligand stabilization and O-O bond activation (By similarity). 
SITE   84    84  1     Influences the redox potential of the prosthetic heme and FAD groups (By similarity). 
SITE   388   388  1     Influences the redox potential of the prosthetic heme and FAD groups (By similarity). 
MOD_RES   22    22        Phosphothreonine. 
MOD_RES   210   210        Phosphoserine. 
VARIANT   153   153  1     D -> E (in strain: JM43). 
VARIANT   345   345  1     N -> D (in strain: JM43). 
VARIANT   365   365  1     L -> V (in strain: JM43). 
Sequence information
Length: 399 AA [This is the length of the unprocessed precursor] Molecular weight: 44646 Da [This is the MW of the unprocessed precursor] CRC64: 8AF1DE3280220D56 [This is a checksum on the sequence]
        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 

P39676 in FASTA format

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