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P05373 (HEM2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Delta-aminolevulinic acid dehydratase

Short name=ALADH
EC=4.2.1.24
Alternative name(s):
Porphobilinogen synthase
Gene names
Name:HEM2
Ordered Locus Names:YGL040C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactor

Binds 1 zinc ion per monomer. Ref.10

Enzyme regulation

Inhibited by divalent lead ions. Ref.9

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.

Subunit structure

Homooctamer. Ref.9 Ref.13

Miscellaneous

Present with 11600 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ALADH family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Delta-aminolevulinic acid dehydratase
PRO_0000140534

Sites

Active site2101Schiff-base intermediate with substrate Ref.9 Ref.10 Ref.12 Ref.13
Active site2631Schiff-base intermediate with substrate Ref.9 Ref.10 Ref.12 Ref.13
Metal binding1331Zinc; catalytic
Metal binding1351Zinc; catalytic
Metal binding1431Zinc; catalytic
Binding site2201Substrate 1
Binding site2321Substrate 1
Binding site2901Substrate 2
Binding site3291Substrate 2

Amino acid modifications

Modified residue2541Phosphoserine Ref.7

Experimental info

Sequence conflict2911G → D in AAA34669. Ref.1

Secondary structure

...................................................................... 342
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05373 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 72F6EB11008BDF52

FASTA34237,740
        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 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the yeast HEM2 gene and transcriptional regulation of COX5 and COR1 by heme."
Myers A.M., Crivellone M.D., Koerner T.J., Tzagoloff A.
J. Biol. Chem. 262:16822-16829(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
Feuermann M., de Montigny J., Potier S., Souciet J.-L.
Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
Strain: ATCC 204508 / S288c.
[6]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"X-ray structure of 5-aminolaevulinate dehydratase, a hybrid aldolase."
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.
Nat. Struct. Biol. 4:1025-1031(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH LEAD IONS, SUBUNIT, ENZYME REGULATION, ACTIVE SITE.
[10]"The Schiff base complex of yeast 5-aminolaevulinic acid dehydratase with laevulinic acid."
Erskine P.T., Newbold R., Roper J., Coker A., Warren M.J., Shoolingin-Jordan P.M., Wood S.P., Cooper J.B.
Protein Sci. 8:1250-1256(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH LAEVULINIC ACID AND ZINC IONS, COFACTOR, ACTIVE SITE.
[11]"MAD analyses of yeast 5-aminolaevulinate dehydratase: their use in structure determination and in defining the metal-binding sites."
Erskine P.T., Duke E.M., Tickle I.J., Senior N.M., Warren M.J., Cooper J.B.
Acta Crystallogr. D 56:421-430(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH MERCURY IONS.
[12]"The X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with two diacid inhibitors."
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.
FEBS Lett. 503:196-200(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEXES WITH ZINC IONS; 4-OXOSEBACIC ACID AND 4,7-DIOXOSEBACIC ACID, ACTIVE SITE.
[13]"The X-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with substrate and three inhibitors."
Erskine P.T., Newbold R., Brindley A.A., Wood S.P., Shoolingin-Jordan P.M., Warren M.J., Cooper J.B.
J. Mol. Biol. 312:133-141(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEXES WITH ZINC IONS; 5-AMINOLAEVULINIC ACID AND SUBSTRATE ANALOGS, ACTIVE SITE, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03493 Genomic DNA. Translation: AAA34669.1.
Z72562 Genomic DNA. Translation: CAA96742.1.
AY692744 Genomic DNA. Translation: AAT92763.1.
BK006941 Genomic DNA. Translation: DAA08060.1.
PIRS64042.
RefSeqNP_011475.1. NM_001180905.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AW5X-ray2.30A1-340[»]
1EB3X-ray1.75A1-340[»]
1GJPX-ray1.80A1-340[»]
1H7NX-ray1.60A1-342[»]
1H7OX-ray1.75A1-341[»]
1H7PX-ray1.64A1-342[»]
1H7RX-ray2.00A1-342[»]
1OHLX-ray1.60A1-342[»]
1QMLX-ray3.00A1-342[»]
1QNVX-ray2.50A1-342[»]
1W31X-ray1.90A1-342[»]
1YLVX-ray2.15A1-342[»]
ProteinModelPortalP05373.
SMRP05373. Positions 1-340.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33206. 63 interactions.
DIPDIP-4311N.
IntActP05373. 4 interactions.
MINTMINT-476599.
STRING4932.YGL040C.

Proteomic databases

PaxDbP05373.
PeptideAtlasP05373.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL040C; YGL040C; YGL040C.
GeneID852842.
KEGGsce:YGL040C.

Organism-specific databases

CYGDYGL040c.
SGDS000003008. HEM2.

Phylogenomic databases

eggNOGCOG0113.
GeneTreeENSGT00390000006998.
HOGENOMHOG000020323.
KOK01698.
OMAIITYFTP.
OrthoDBEOG779P7W.

Enzyme and pathway databases

BioCycYEAST:YGL040C-MONOMER.
UniPathwayUPA00251; UER00318.

Gene expression databases

GenevestigatorP05373.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERPTHR11458. PTHR11458. 1 hit.
PfamPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSPR00144. DALDHYDRTASE.
SMARTSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05373.
NextBio972420.
PROP05373.

Entry information

Entry nameHEM2_YEAST
AccessionPrimary (citable) accession number: P05373
Secondary accession number(s): D6VU99
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1996
Last modified: March 19, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways