Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P06214

- HEM2_RAT

UniProt

P06214 - HEM2_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Delta-aminolevulinic acid dehydratase

Gene

Alad

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 By similarity.By similarity

Catalytic activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactori

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.By similarity

Enzyme 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi122 – 1221Zinc 1; catalyticBy similarity
Metal bindingi124 – 1241Zinc 1; catalyticBy similarity
Metal bindingi131 – 1311Zinc 2By similarity
Metal bindingi132 – 1321Zinc 1; catalyticBy similarity
Active sitei199 – 1991Schiff-base intermediate with substrateBy similarity
Binding sitei209 – 2091Substrate 1By similarity
Binding sitei221 – 2211Substrate 1By similarity
Metal bindingi223 – 2231Zinc 2By similarity
Active sitei252 – 2521Schiff-base intermediate with substrateBy similarity
Binding sitei279 – 2791Substrate 2By similarity
Binding sitei318 – 3181Substrate 2By similarity

GO - Molecular functioni

  1. lead ion binding Source: UniProtKB
  2. porphobilinogen synthase activity Source: UniProtKB
  3. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cellular response to lead ion Source: RGD
  2. heme biosynthetic process Source: UniProtKB
  3. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
  4. response to activity Source: RGD
  5. response to aluminum ion Source: RGD
  6. response to amino acid Source: RGD
  7. response to arsenic-containing substance Source: RGD
  8. response to cadmium ion Source: RGD
  9. response to cobalt ion Source: RGD
  10. response to drug Source: RGD
  11. response to ethanol Source: RGD
  12. response to fatty acid Source: RGD
  13. response to glucocorticoid Source: RGD
  14. response to herbicide Source: RGD
  15. response to hormone Source: RGD
  16. response to hypoxia Source: RGD
  17. response to inorganic substance Source: RGD
  18. response to ionizing radiation Source: RGD
  19. response to iron ion Source: RGD
  20. response to lead ion Source: RGD
  21. response to lipopolysaccharide Source: RGD
  22. response to mercury ion Source: RGD
  23. response to metal ion Source: RGD
  24. response to methylmercury Source: RGD
  25. response to nutrient Source: RGD
  26. response to nutrient levels Source: RGD
  27. response to organic cyclic compound Source: RGD
  28. response to organic substance Source: RGD
  29. response to oxidative stress Source: RGD
  30. response to platinum ion Source: RGD
  31. response to selenium ion Source: RGD
  32. response to toxic substance Source: RGD
  33. response to vitamin Source: RGD
  34. response to vitamin B1 Source: RGD
  35. response to vitamin E Source: RGD
  36. response to zinc ion Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

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:Alad
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 5

Organism-specific databases

RGDi2083. Alad.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RGD
  2. extracellular space Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Delta-aminolevulinic acid dehydratasePRO_0000140530Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei199 – 1991N6-succinyllysineBy similarity
Modified residuei215 – 2151PhosphoserineBy similarity
Modified residuei252 – 2521N6-succinyllysineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP06214.
PRIDEiP06214.

PTM databases

PhosphoSiteiP06214.

Expressioni

Gene expression databases

GenevestigatoriP06214.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi247413. 1 interaction.
MINTiMINT-4567662.
STRINGi10116.ENSRNOP00000020625.

Structurei

3D structure databases

ProteinModelPortaliP06214.
SMRiP06214. Positions 5-328.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiCOG0113.
GeneTreeiENSGT00390000006998.
HOGENOMiHOG000020323.
HOVERGENiHBG001222.
InParanoidiP06214.
KOiK01698.
OMAiDHPTACY.
OrthoDBiEOG751NFP.
PhylomeDBiP06214.
TreeFamiTF300665.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[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.

P06214-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHHQSVLHSG YFHPLLRAWQ TTPSTVSATN LIYPIFVTDV PDDVQPIASL
60 70 80 90 100
PGVARYGVNQ LEEMLRPLVE AGLRCVLIFG VPSRVPKDEQ GSAADSEDSP
110 120 130 140 150
TIEAVRLLRK TFPTLLVACD VCLCPYTSHG HCGLLSENGA FLAEESRQRL
160 170 180 190 200
AEVALAYAKA GCQVVAPSDM MDGRVEAIKA ALLKHGLGNR VSVMSYSAKF
210 220 230 240 250
ASCFYGPFRD AAQSSPAFGD RRCYQLPPGA RGLALRAVAR DIQEGADILM
260 270 280 290 300
VKPGLPYLDM VQEVKDKHPE LPLAVYQVSG EFAMLWHGAK AGAFDLRTAV
310 320 330
LESMTAFRRA GADIIITYFA PQLLKWLKEE
Length:330
Mass (Da):36,032
Last modified:January 1, 1988 - v1
Checksum:i617F6E85B647AB25
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04959 mRNA. Translation: CAA28621.1.
BC061806 mRNA. Translation: AAH61806.1.
PIRiA24724.
RefSeqiNP_037031.1. NM_012899.2.
XP_006238296.1. XM_006238234.2.
XP_006238297.1. XM_006238235.1.
UniGeneiRn.3941.

Genome annotation databases

EnsembliENSRNOT00000020625; ENSRNOP00000020625; ENSRNOG00000015206.
GeneIDi25374.
KEGGirno:25374.
UCSCiRGD:2083. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04959 mRNA. Translation: CAA28621.1 .
BC061806 mRNA. Translation: AAH61806.1 .
PIRi A24724.
RefSeqi NP_037031.1. NM_012899.2.
XP_006238296.1. XM_006238234.2.
XP_006238297.1. XM_006238235.1.
UniGenei Rn.3941.

3D structure databases

ProteinModelPortali P06214.
SMRi P06214. Positions 5-328.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 247413. 1 interaction.
MINTi MINT-4567662.
STRINGi 10116.ENSRNOP00000020625.

PTM databases

PhosphoSitei P06214.

Proteomic databases

PaxDbi P06214.
PRIDEi P06214.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000020625 ; ENSRNOP00000020625 ; ENSRNOG00000015206 .
GeneIDi 25374.
KEGGi rno:25374.
UCSCi RGD:2083. rat.

Organism-specific databases

CTDi 210.
RGDi 2083. Alad.

Phylogenomic databases

eggNOGi COG0113.
GeneTreei ENSGT00390000006998.
HOGENOMi HOG000020323.
HOVERGENi HBG001222.
InParanoidi P06214.
KOi K01698.
OMAi DHPTACY.
OrthoDBi EOG751NFP.
PhylomeDBi P06214.
TreeFami TF300665.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00318 .

Miscellaneous databases

NextBioi 606397.
PROi P06214.

Gene expression databases

Genevestigatori P06214.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view ]
PANTHERi PTHR11458. PTHR11458. 1 hit.
Pfami PF00490. ALAD. 1 hit.
[Graphical view ]
PIRSFi PIRSF001415. Porphbilin_synth. 1 hit.
PRINTSi PR00144. DALDHYDRTASE.
SMARTi SM01004. ALAD. 1 hit.
[Graphical view ]
PROSITEi PS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of rat liver delta-aminolevulinic acid dehydratase cDNA."
    Bishop T.R., Frelin L.P., Boyer S.H.
    Nucleic Acids Res. 14:10115-10115(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "Isolation of a rat liver delta-aminolevulinate dehydrase (ALAD) cDNA clone: evidence for unequal ALAD gene dosage among inbred mouse strains."
    Bishop T.R., Cohen P.J., Boyer S.H., Noyes A.N., Frelin L.P.
    Proc. Natl. Acad. Sci. U.S.A. 83:5568-5572(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-45.
  4. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 56-84 AND 200-209, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.

Entry informationi

Entry nameiHEM2_RAT
AccessioniPrimary (citable) accession number: P06214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: October 29, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3