Reviewed, UniProtKB/Swiss-Prot P05373 (HEM2_YEAST)

Names and origin

Protein names

Recommended 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

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

General annotation (Comments)

Catalytic activity	2 5-aminolevulinate = porphobilinogen + 2 H2O.
Cofactor	Zinc.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Subunit structure	Homooctamer.
Miscellaneous	Present with 11600 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the ALADH family.

Ontologies

Keywords
Biological process	Heme biosynthesis Porphyrin biosynthesis
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	heme biosynthetic process Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	identical protein binding Inferred from physical interaction. Source: IntAct porphobilinogen synthase activity Ref.1 Inferred from direct assay. Source: SGD zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-8239,EBI-8239
SRP1	Q02821	1	EBI-8239,EBI-1797
TEM1	P38987	1	EBI-8239,EBI-19113

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 342

342

Delta-aminolevulinic acid dehydratase

PRO_0000140534

Sites

Active site

263

1

Metal binding

133

1

Zinc; catalytic

Metal binding

135

1

Zinc; catalytic

Metal binding

143

1

Zinc; catalytic

Amino acid modifications

Modified residue

254

1

Phosphoserine Ref.6

Experimental info

Sequence conflict

291

1

G → D in AAA34669. Ref.1

Secondary structure

1

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342

Helix Strand Turn

Details...

Helix

14 – 16

3

Helix

19 – 21

3

Helix

27 – 30

4

Beta strand

32 – 34

3

Helix

38 – 40

3

Beta strand

41 – 50

10

Beta strand

54 – 56

3

Beta strand

64 – 66

3

Turn

68 – 70

3

Helix

71 – 80

10

Beta strand

85 – 91

7

Helix

103 – 106

4

Helix

111 – 122

12

Beta strand

126 – 132

7

Turn

135 – 137

3

Beta strand

138 – 140

3

Beta strand

150 – 152

3

Helix

154 – 170

17

Beta strand

174 – 178

5

Helix

185 – 195

11

Turn

199 – 201

3

Beta strand

203 – 211

9

Helix

242 – 254

13

Beta strand

258 – 264

7

Helix

266 – 268

3

Helix

269 – 278

10

Turn

279 – 281

3

Beta strand

284 – 287

4

Helix

290 – 301

12

Helix

307 – 321

15

Beta strand

324 – 327

4

Helix

331 – 337

7

Sequences

	Sequence		Length	Mass (Da)
	P05373-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 72F6EB11008BDF52	FASTA	342	37,740
	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

References

	« Hide 'large scale' referencesShow '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: 2445751] [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. , 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.
[3]	"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.
[4]	"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: 9234674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41. Strain: ATCC 204508 / S288c.
[5]	"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].
[6]	"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 SER-254, MASS SPECTROMETRY.
[7]	"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: 9406553] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[8]	"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: 10386874] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
[9]	"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: 10739915] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[10]	"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: 11513881] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
[11]	"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: 11545591] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J03493 Genomic DNA. Translation: AAA34669.1.
Z72562 Genomic DNA. Translation: CAA96742.1.
AY692744 Genomic DNA. Translation: AAT92763.1.

PIR

S64042.

RefSeq

NP_011475.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AW5	X-ray	2.30	A	1-340	[»]
1EB3	X-ray	1.75	A	1-340	[»]
1GJP	X-ray	1.80	A	1-340	[»]
1H7N	X-ray	1.60	A	1-342	[»]
1H7O	X-ray	1.75	A	1-341	[»]
1H7P	X-ray	1.64	A	1-342	[»]
1H7R	X-ray	2.00	A	1-342	[»]
1OHL	X-ray	1.60	A	1-342	[»]
1QML	X-ray	3.00	A	1-342	[»]
1QNV	X-ray	2.50	A	1-342	[»]
1W31	X-ray	1.90	A	1-342	[»]
1YLV	X-ray	2.15	A	1-342	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:4311N.

IntAct

P05373. 6 interactions.

Proteomic databases

PeptideAtlas

P05373.

Genome annotation databases

Ensembl

YGL040C. Saccharomyces cerevisiae. [Contig view]

GeneID

852842.

GenomeReviews

Gene locus YGL040C in contig Y13135_GR.

KEGG

sce:YGL040C.

NMPDR

fig|4932.3.peg.2582.

Organism-specific databases

CYGD

YGL040c.

SGD

S000003008. HEM2.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P05373.

OMA

P05373. AESTPQF.

Enzyme and pathway databases

BRENDA

4.2.1.24. 250.

Gene expression databases

ArrayExpress

P05373.

GermOnline

YGL040C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR001731. 4pyrrol_synth_porphobiln_synth.
IPR013785. Aldolase_TIM.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

PANTHER

PTHR11458. AlaD_dehydratase. 1 hit.

Pfam

PF00490. ALAD. 1 hit.
[Graphical view]

PIRSF

PIRSF001415. Porphbilin_synth. 1 hit.

PRINTS

PR00144. DALDHYDRTASE.

ProDom

PD002304. AlaD_dehydratase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

972420.

Entry information

Entry name

HEM2_YEAST

Accession

Primary (citable) accession number: P05373

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)