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Protein

Delta-aminolevulinic acid dehydratase

Gene

HEM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per monomer.1 Publication

Enzyme regulationi

Inhibited by divalent lead ions.1 Publication

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Delta-aminolevulinic acid dehydratase (HEM2)
  2. Porphobilinogen deaminase (HEM3)
  3. Uroporphyrinogen-III synthase (HEM4)
  4. Uroporphyrinogen decarboxylase (HEM12)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi133Zinc; catalytic1
Metal bindingi135Zinc; catalytic1
Metal bindingi143Zinc; catalytic1
Active sitei210Schiff-base intermediate with substrate1
Binding sitei220Substrate 11
Binding sitei232Substrate 11
Active sitei263Schiff-base intermediate with substrate1
Binding sitei290Substrate 21
Binding sitei329Substrate 21

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YGL040C-MONOMER.
BRENDAi4.2.1.24. 984.
ReactomeiR-SCE-189451. Heme biosynthesis.
R-SCE-6798695. Neutrophil degranulation.
UniPathwayiUPA00251; UER00318.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:HEM2
Ordered Locus Names:YGL040C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL040C.
SGDiS000003008. HEM2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001405341 – 342Delta-aminolevulinic acid dehydrataseAdd BLAST342

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei254PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP05373.
PRIDEiP05373.

PTM databases

iPTMnetiP05373.

Interactioni

Subunit structurei

Homooctamer.4 Publications

Protein-protein interaction databases

BioGridi33206. 62 interactors.
DIPiDIP-4311N.
IntActiP05373. 4 interactors.
MINTiMINT-476599.

Structurei

Secondary structure

1342
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 16Combined sources3
Helixi19 – 21Combined sources3
Beta strandi22 – 24Combined sources3
Helixi25 – 30Combined sources6
Beta strandi32 – 34Combined sources3
Helixi38 – 40Combined sources3
Beta strandi41 – 50Combined sources10
Beta strandi54 – 56Combined sources3
Beta strandi58 – 60Combined sources3
Beta strandi64 – 66Combined sources3
Helixi68 – 80Combined sources13
Beta strandi85 – 91Combined sources7
Helixi103 – 106Combined sources4
Helixi111 – 122Combined sources12
Beta strandi126 – 132Combined sources7
Turni135 – 137Combined sources3
Beta strandi138 – 140Combined sources3
Beta strandi142 – 144Combined sources3
Beta strandi150 – 152Combined sources3
Helixi154 – 171Combined sources18
Beta strandi174 – 178Combined sources5
Helixi185 – 195Combined sources11
Turni199 – 201Combined sources3
Beta strandi203 – 211Combined sources9
Beta strandi213 – 215Combined sources3
Helixi217 – 223Combined sources7
Beta strandi228 – 230Combined sources3
Turni233 – 235Combined sources3
Helixi242 – 254Combined sources13
Beta strandi258 – 265Combined sources8
Helixi266 – 268Combined sources3
Helixi269 – 278Combined sources10
Turni279 – 281Combined sources3
Beta strandi284 – 288Combined sources5
Helixi290 – 301Combined sources12
Helixi307 – 320Combined sources14
Beta strandi324 – 328Combined sources5
Helixi331 – 337Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP05373.
SMRiP05373.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05373.

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000006998.
HOGENOMiHOG000020323.
InParanoidiP05373.
KOiK01698.
OMAiQFLDWLD.
OrthoDBiEOG092C32OH.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05373-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHTAEFLETE PTEISSVLAG GYNHPLLRQW QSERQLTKNM LIFPLFISDN
60 70 80 90 100
PDDFTEIDSL PNINRIGVNR LKDYLKPLVA KGLRSVILFG VPLIPGTKDP
110 120 130 140 150
VGTAADDPAG PVIQGIKFIR EYFPELYIIC DVCLCEYTSH GHCGVLYDDG
160 170 180 190 200
TINRERSVSR LAAVAVNYAK AGAHCVAPSD MIDGRIRDIK RGLINANLAH
210 220 230 240 250
KTFVLSYAAK FSGNLYGPFR DAACSAPSNG DRKCYQLPPA GRGLARRALE
260 270 280 290 300
RDMSEGADGI IVKPSTFYLD IMRDASEICK DLPICAYHVS GEYAMLHAAA
310 320 330 340
EKGVVDLKTI AFESHQGFLR AGARLIITYL APEFLDWLDE EN
Length:342
Mass (Da):37,740
Last modified:October 1, 1996 - v2
Checksum:i72F6EB11008BDF52
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti291G → D in AAA34669 (PubMed:2445751).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03493 Genomic DNA. Translation: AAA34669.1.
Z72562 Genomic DNA. Translation: CAA96742.1.
AY692744 Genomic DNA. Translation: AAT92763.1.
BK006941 Genomic DNA. Translation: DAA08060.1.
PIRiS64042.
RefSeqiNP_011475.1. NM_001180905.1.

Genome annotation databases

EnsemblFungiiYGL040C; YGL040C; YGL040C.
GeneIDi852842.
KEGGisce:YGL040C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03493 Genomic DNA. Translation: AAA34669.1.
Z72562 Genomic DNA. Translation: CAA96742.1.
AY692744 Genomic DNA. Translation: AAT92763.1.
BK006941 Genomic DNA. Translation: DAA08060.1.
PIRiS64042.
RefSeqiNP_011475.1. NM_001180905.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP05373.
SMRiP05373.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33206. 62 interactors.
DIPiDIP-4311N.
IntActiP05373. 4 interactors.
MINTiMINT-476599.

PTM databases

iPTMnetiP05373.

Proteomic databases

MaxQBiP05373.
PRIDEiP05373.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL040C; YGL040C; YGL040C.
GeneIDi852842.
KEGGisce:YGL040C.

Organism-specific databases

EuPathDBiFungiDB:YGL040C.
SGDiS000003008. HEM2.

Phylogenomic databases

GeneTreeiENSGT00390000006998.
HOGENOMiHOG000020323.
InParanoidiP05373.
KOiK01698.
OMAiQFLDWLD.
OrthoDBiEOG092C32OH.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.
BioCyciYEAST:YGL040C-MONOMER.
BRENDAi4.2.1.24. 984.
ReactomeiR-SCE-189451. Heme biosynthesis.
R-SCE-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP05373.
PROiP05373.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR001731. ALAD.
IPR030656. ALAD_AS.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHEM2_YEAST
AccessioniPrimary (citable) accession number: P05373
Secondary accession number(s): D6VU99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 171 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 11600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.