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Protein

Delta-aminolevulinic acid dehydratase

Gene

Alad

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 (By similarity).By similarity

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactori

Zn2+By similarityNote: Binds 8 zinc ions per octamer. Requires four zinc ions per octamer for full catalytic activity. Can bind up to 2 zinc ions per subunit.By similarity

Activity regulationi

Can alternate between a fully active homooctamer and a low-activity homohexamer. A bound magnesium ion may promote the assembly of the fully active homooctamer. The magnesium-binding site is absent in the low-activity homohexamer. Inhibited by compounds that favor the hexameric state. Inhibited by divalent lead ions. The lead ions partially displace the zinc cofactor (By similarity).By similarity

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 (Alad)
  2. Porphobilinogen deaminase (Hmbs)
  3. Uroporphyrinogen-III synthase (Uros)
  4. Uroporphyrinogen decarboxylase (Urod)
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 bindingi122Zinc 1; catalyticBy similarity1
Metal bindingi124Zinc 1; catalyticBy similarity1
Metal bindingi131Zinc 2By similarity1
Metal bindingi132Zinc 1; catalyticBy similarity1
Active sitei199Schiff-base intermediate with substrateBy similarity1
Binding sitei209Substrate 1By similarity1
Binding sitei221Substrate 1By similarity1
Metal bindingi223Zinc 2By similarity1
Active sitei252Schiff-base intermediate with substrateBy similarity1
Binding sitei279Substrate 2By similarity1
Binding sitei318Substrate 2By similarity1

GO - Molecular functioni

  • identical protein binding Source: MGI
  • porphobilinogen synthase activity Source: MGI
  • proteasome core complex binding Source: MGI
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionAllosteric enzyme, Lyase
Biological processHeme biosynthesis, Porphyrin biosynthesis
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-189451 Heme biosynthesis
R-MMU-6798695 Neutrophil degranulation
UniPathwayi
UPA00251;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:Alad
Synonyms:Lv
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:96853 Alad

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001405281 – 330Delta-aminolevulinic acid dehydrataseAdd BLAST330

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei199N6-succinyllysineCombined sources1
Modified residuei215PhosphoserineCombined sources1
Modified residuei252N6-succinyllysineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP10518
MaxQBiP10518
PaxDbiP10518
PeptideAtlasiP10518
PRIDEiP10518

2D gel databases

REPRODUCTION-2DPAGEiP10518
SWISS-2DPAGEiP10518

PTM databases

iPTMnetiP10518
PhosphoSitePlusiP10518
SwissPalmiP10518

Expressioni

Gene expression databases

BgeeiENSMUSG00000028393 Expressed in 286 organ(s), highest expression level in liver
CleanExiMM_ALAD
GenevisibleiP10518 MM

Interactioni

Subunit structurei

Homooctamer; active form. Homohexamer; low activity form (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201229, 2 interactors
IntActiP10518, 6 interactors
MINTiP10518
STRINGi10090.ENSMUSP00000030090

Structurei

Secondary structure

1330
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP10518
SMRiP10518
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10518

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiKOG2794 Eukaryota
COG0113 LUCA
GeneTreeiENSGT00390000006998
HOGENOMiHOG000020323
HOVERGENiHBG001222
InParanoidiP10518
KOiK01698
OMAiYQMDYAN
OrthoDBiEOG091G0FMX
PhylomeDBiP10518
TreeFamiTF300665

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR001731 ALAD
IPR030656 ALAD_AS
IPR013785 Aldolase_TIM
PANTHERiPTHR11458 PTHR11458, 1 hit
PfamiView protein in Pfam
PF00490 ALAD, 1 hit
PIRSFiPIRSF001415 Porphbilin_synth, 1 hit
PRINTSiPR00144 DALDHYDRTASE
SMARTiView protein in SMART
SM01004 ALAD, 1 hit
PROSITEiView protein in PROSITE
PS00169 D_ALA_DEHYDRATASE, 1 hit

Sequencei

Sequence statusi: Complete.

P10518-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHHQSVLHSG YFHPLLRSWQ TAASTVSASN LIYPIFVTDV PDDVQPIASL
60 70 80 90 100
PGVARYGVNQ LEEMLRPLVE AGLRCVLIFG VPSRVPKDEQ GSAADSEDSP
110 120 130 140 150
TIEAVRLLRK TFPSLLVACD VCLCPYTSHG HCGLLSENGA FLAEESRQRL
160 170 180 190 200
AEVALAYAKA GCQVVAPSDM MDGRVEAIKA ALLKHGLGNR VSVMSYSAKF
210 220 230 240 250
ASCFYGPFRD AAQSSPAFGD RRCYQLPPGA RGLALRAVAR DIQEGADMLM
260 270 280 290 300
VKPGLPYLDM VREVKDKHPE LPLAVYQVSG EFAMLWHGAQ AGAFDLRTAV
310 320 330
LETMTAFRRA GADIIITYFA PQLLKWLKEE
Length:330
Mass (Da):36,024
Last modified:July 1, 1989 - v1
Checksum:i84052DC911C153EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13752 mRNA Translation: CAA32015.1
AK032908 mRNA Translation: BAC28080.1
AK167673 mRNA Translation: BAE39722.1
AK168119 mRNA Translation: BAE40090.1
AK168132 mRNA Translation: BAE40101.1
BC055930 mRNA Translation: AAH55930.1
CCDSiCCDS18243.1
PIRiS03187
RefSeqiNP_001263375.1, NM_001276446.1
NP_032551.3, NM_008525.4
XP_006537702.1, XM_006537639.2
UniGeneiMm.6988

Genome annotation databases

EnsembliENSMUST00000030090; ENSMUSP00000030090; ENSMUSG00000028393
ENSMUST00000107444; ENSMUSP00000103068; ENSMUSG00000028393
GeneIDi17025
KEGGimmu:17025
UCSCiuc008tez.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13752 mRNA Translation: CAA32015.1
AK032908 mRNA Translation: BAC28080.1
AK167673 mRNA Translation: BAE39722.1
AK168119 mRNA Translation: BAE40090.1
AK168132 mRNA Translation: BAE40101.1
BC055930 mRNA Translation: AAH55930.1
CCDSiCCDS18243.1
PIRiS03187
RefSeqiNP_001263375.1, NM_001276446.1
NP_032551.3, NM_008525.4
XP_006537702.1, XM_006537639.2
UniGeneiMm.6988

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Z0IX-ray3.20A/B1-330[»]
2Z1BX-ray3.30A/B/C/D1-330[»]
ProteinModelPortaliP10518
SMRiP10518
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201229, 2 interactors
IntActiP10518, 6 interactors
MINTiP10518
STRINGi10090.ENSMUSP00000030090

PTM databases

iPTMnetiP10518
PhosphoSitePlusiP10518
SwissPalmiP10518

2D gel databases

REPRODUCTION-2DPAGEiP10518
SWISS-2DPAGEiP10518

Proteomic databases

EPDiP10518
MaxQBiP10518
PaxDbiP10518
PeptideAtlasiP10518
PRIDEiP10518

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030090; ENSMUSP00000030090; ENSMUSG00000028393
ENSMUST00000107444; ENSMUSP00000103068; ENSMUSG00000028393
GeneIDi17025
KEGGimmu:17025
UCSCiuc008tez.2 mouse

Organism-specific databases

CTDi210
MGIiMGI:96853 Alad

Phylogenomic databases

eggNOGiKOG2794 Eukaryota
COG0113 LUCA
GeneTreeiENSGT00390000006998
HOGENOMiHOG000020323
HOVERGENiHBG001222
InParanoidiP10518
KOiK01698
OMAiYQMDYAN
OrthoDBiEOG091G0FMX
PhylomeDBiP10518
TreeFamiTF300665

Enzyme and pathway databases

UniPathwayi
UPA00251;UER00318

ReactomeiR-MMU-189451 Heme biosynthesis
R-MMU-6798695 Neutrophil degranulation

Miscellaneous databases

ChiTaRSiAlad mouse
EvolutionaryTraceiP10518
PROiPR:P10518
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028393 Expressed in 286 organ(s), highest expression level in liver
CleanExiMM_ALAD
GenevisibleiP10518 MM

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR001731 ALAD
IPR030656 ALAD_AS
IPR013785 Aldolase_TIM
PANTHERiPTHR11458 PTHR11458, 1 hit
PfamiView protein in Pfam
PF00490 ALAD, 1 hit
PIRSFiPIRSF001415 Porphbilin_synth, 1 hit
PRINTSiPR00144 DALDHYDRTASE
SMARTiView protein in SMART
SM01004 ALAD, 1 hit
PROSITEiView protein in PROSITE
PS00169 D_ALA_DEHYDRATASE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiHEM2_MOUSE
AccessioniPrimary (citable) accession number: P10518
Secondary accession number(s): Q3THV6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 12, 2018
This is version 158 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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