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UniProtKB/Swiss-Prot entry P05373


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

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Entry information
Entry name HEM2_YEAST
Primary accession number P05373
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 98)
Name and origin of the protein
Protein name Delta-aminolevulinic acid dehydratase
Synonyms ALADH
EC 4.2.1.24
Porphobilinogen synthase
Gene name
Name: HEM2
OrderedLocusNames: YGL040C
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].
PubMed=2445751 [NCBI, ExPASy, EBI, Israel, Japan]
Myers A.M., Crivellone M.D., Koerner T.J., Tzagoloff A.;
"Characterization of the yeast HEM2 gene and transcriptional regulation of COX5 and COR1 by heme.";
J. Biol. Chem. 262:16822-16829(1987).
[2]
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).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/(SICI)1097-0061(199707)13:9<861::AID-YEA125>3.3.CO;2-0; PubMed=9234674 [NCBI, ExPASy, EBI, Israel, Japan]
Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
"The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
Yeast 13:861-869(1997).
[5]
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, 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 7:1389-1396(2008).
[7]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1038/nsb1297-1025; PubMed=9406553 [NCBI, ExPASy, EBI, Israel, Japan]
Erskine P.T., Senior N., Awan S., Lambert R., Lewis G., Tickle I.J., Sarwar M., Spencer P., Thomas P., Warren M.J., Shoolingin-Jordan P.M., Wood S.P., Cooper J.B.;
"X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase.";
Nat. Struct. Biol. 4:1025-1031(1997).
[8]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
PubMed=10386874 [NCBI, ExPASy, EBI, Israel, Japan]
Erskine P.T., Newbold R., Roper J., Coker A., Warren M.J., Shoolingin-Jordan P.M., Wood S.P., Cooper J.B.;
"The Schiff base complex of yeast 5-aminolaevulinic acid dehydratase with laevulinic acid.";
Protein Sci. 8:1250-1256(1999).
[9]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1107/S0907444900000597; PubMed=10739915 [NCBI, ExPASy, EBI, Israel, Japan]
Erskine P.T., Duke E.M., Tickle I.J., Senior N.M., Warren M.J., Cooper J.B.;
"MAD analyses of yeast 5-aminolaevulinate dehydratase: their use in structure determination and in defining the metal-binding sites.";
Acta Crystallogr. D 56:421-430(2000).
[10]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
DOI=10.1016/S0014-5793(01)02721-1; PubMed=11513881 [NCBI, ExPASy, EBI, Israel, Japan]
Erskine P.T., Coates L., Newbold R., Brindley A.A., Stauffer F., Wood S.P., Warren M.J., Cooper J.B., Shoolingin-Jordan P.M., Neier R.;
"The X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with two diacid inhibitors.";
FEBS Lett. 503:196-200(2001).
[11]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
DOI=10.1006/jmbi.2001.4947; PubMed=11545591 [NCBI, ExPASy, EBI, Israel, Japan]
Erskine P.T., Newbold R., Brindley A.A., Wood S.P., Shoolingin-Jordan P.M., Warren M.J., Cooper J.B.;
"The X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with substrate and three inhibitors.";
J. Mol. Biol. 312:133-141(2001).
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
J03493; AAA34669.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z72562; CAA96742.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY692744; AAT92763.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64042; S64042.
RefSeq NP_011475.1; -.
3D structure databases
PDB
1AW5; X-ray; 2.30 A; A=1-340.[ExPASy / RCSB / EBI]
1EB3; X-ray; 1.75 A; A=1-340.[ExPASy / RCSB / EBI]
1GJP; X-ray; 1.80 A; A=1-340.[ExPASy / RCSB / EBI]
1H7N; X-ray; 1.60 A; A=1-342.[ExPASy / RCSB / EBI]
1H7O; X-ray; 1.75 A; A=1-341.[ExPASy / RCSB / EBI]
1H7P; X-ray; 1.64 A; A=1-342.[ExPASy / RCSB / EBI]
1H7R; X-ray; 2.00 A; A=1-342.[ExPASy / RCSB / EBI]
1OHL; X-ray; 1.60 A; A=1-342.[ExPASy / RCSB / EBI]
1QML; X-ray; 3.00 A; A=1-342.[ExPASy / RCSB / EBI]
1QNV; X-ray; 2.50 A; A=1-342.[ExPASy / RCSB / EBI]
1W31; X-ray; 1.90 A; A=1-342.[ExPASy / RCSB / EBI]
1YLV; X-ray; 2.15 A; A=1-342.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AW5; -.
1EB3; -.
1GJP; -.
1H7N; -.
1H7O; -.
1H7P; -.
1H7R; -.
1OHL; -.
1QML; -.
1QNV; -.
1W31; -.
1YLV; -.
ModBase P05373.
Protein-protein interaction databases
DIP DIP:4311N; -.
IntAct P05373; -.
Organism-specific databases
CYGD YGL040c; -.
SGD S000003008; HEM2.
Yeast-GFP YGL040C.
Gene expression databases
ArrayExpress P05373; -.
GermOnline YGL040C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0004655; Molecular function: porphobilinogen synthase activity (inferred from mutant phenotype from SGD).
GO:0006783; Biological process: heme biosynthetic process (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001731; 4pyrrol_synth_porphobiln_synth.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
PANTHER PTHR11458; AlaD_dehydratase; 1.
Pfam PF00490; ALAD; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001415; Porphbilin_synth; 1.
PRINTS PR00144; DALDHYDRTASE.
ProDom PD002304; AlaD_dehydratase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00169; D_ALA_DEHYDRATASE; 1.
BLOCKS P05373.
ProtoNet P05373.
Proteomic databases
PeptideAtlas P05373; -.
Genome annotation databases
Ensembl YGL040C; Saccharomyces cerevisiae. [Contig view]
GeneID 852842; -.
GenomeReviews Y13135_GR; YGL040C.
KEGG sce:YGL040C; -.
NMPDR fig|4932.3.peg.2582; -.
Phylogenomic databases
HOGENOM P05373; -.
Other
LinkHub P05373; -.
NextBio 972420; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Heme biosynthesis; Lyase; Metal-binding; Phosphoprotein; Porphyrin biosynthesis; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   342  342     Delta-aminolevulinic acid dehydratase. PRO_0000140534
ACT_SITE   263   263         
METAL   133   133        Zinc; catalytic. 
METAL   135   135        Zinc; catalytic. 
METAL   143   143        Zinc; catalytic. 
MOD_RES   254   254        Phosphoserine. 
CONFLICT   291   291        G -> D (in Ref. 1; AAA34669). 
HELIX   14    16  3      
HELIX   19    21  3      
HELIX   27    30  4      
STRAND   32    34  3      
HELIX   38    40  3      
STRAND   41    50  10      
STRAND   54    56  3      
STRAND   64    66  3      
TURN   68    70  3      
HELIX   71    80  10      
STRAND   85    91  7      
HELIX   103   106  4      
HELIX   111   122  12      
STRAND   126   132  7      
TURN   135   137  3      
STRAND   138   140  3      
STRAND   150   152  3      
HELIX   154   170  17      
STRAND   174   178  5      
HELIX   185   195  11      
TURN   199   201  3      
STRAND   203   211  9      
HELIX   242   254  13      
STRAND   258   264  7      
HELIX   266   268  3      
HELIX   269   278  10      
TURN   279   281  3      
STRAND   284   287  4      
HELIX   290   301  12      
HELIX   307   321  15      
STRAND   324   327  4      
HELIX   331   337  7      
Sequence information
Length: 342 AA [This is the length of the unprocessed precursor] Molecular weight: 37740 Da [This is the MW of the unprocessed precursor] CRC64: 72F6EB11008BDF52 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MHTAEFLETE PTEISSVLAG GYNHPLLRQW QSERQLTKNM LIFPLFISDN PDDFTEIDSL 

        70         80         90        100        110        120 
PNINRIGVNR LKDYLKPLVA KGLRSVILFG VPLIPGTKDP VGTAADDPAG PVIQGIKFIR 

       130        140        150        160        170        180 
EYFPELYIIC DVCLCEYTSH GHCGVLYDDG TINRERSVSR LAAVAVNYAK AGAHCVAPSD 

       190        200        210        220        230        240 
MIDGRIRDIK RGLINANLAH KTFVLSYAAK FSGNLYGPFR DAACSAPSNG DRKCYQLPPA 

       250        260        270        280        290        300 
GRGLARRALE RDMSEGADGI IVKPSTFYLD IMRDASEICK DLPICAYHVS GEYAMLHAAA 

       310        320        330        340 
EKGVVDLKTI AFESHQGFLR AGARLIITYL APEFLDWLDE EN 

P05373 in FASTA format

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