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P10518

- HEM2_MOUSE

UniProt

P10518 - HEM2_MOUSE

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Protein

Delta-aminolevulinic acid dehydratase

Gene

Alad

Organism
Mus musculus (Mouse)
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. identical protein binding Source: MGI
  2. lead ion binding Source: UniProtKB
  3. porphobilinogen synthase activity Source: UniProtKB
  4. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cellular response to interleukin-4 Source: MGI
  2. heme biosynthetic process Source: UniProtKB
  3. protein homooligomerization Source: Ensembl
  4. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_203298. Heme biosynthesis.
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
Synonyms:Lv
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:96853. Alad.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. nucleus Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Delta-aminolevulinic acid dehydratasePRO_0000140528Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei199 – 1991N6-succinyllysine1 Publication
Modified residuei215 – 2151Phosphoserine1 Publication
Modified residuei252 – 2521N6-succinyllysine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP10518.
PaxDbiP10518.
PRIDEiP10518.

2D gel databases

REPRODUCTION-2DPAGEP10518.
SWISS-2DPAGEP10518.

PTM databases

PhosphoSiteiP10518.

Expressioni

Gene expression databases

BgeeiP10518.
CleanExiMM_ALAD.
ExpressionAtlasiP10518. baseline and differential.
GenevestigatoriP10518.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP10518. 5 interactions.
MINTiMINT-1869777.

Structurei

Secondary structure

1
330
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 103
Helixi14 – 207
Helixi28 – 303
Beta strandi31 – 4212
Beta strandi44 – 463
Beta strandi48 – 503
Beta strandi54 – 574
Helixi58 – 603
Helixi61 – 644
Helixi66 – 694
Turni70 – 723
Beta strandi75 – 817
Helixi100 – 11112
Beta strandi113 – 1197
Helixi144 – 16017
Beta strandi163 – 1653
Helixi174 – 18310
Turni185 – 1884
Beta strandi192 – 1943
Helixi206 – 2116
Helixi231 – 24111
Helixi242 – 2443
Beta strandi247 – 2548
Helixi255 – 2573
Helixi258 – 26710
Beta strandi273 – 2764
Helixi279 – 29012
Helixi296 – 30914
Beta strandi313 – 3164
Helixi320 – 3267

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z0IX-ray3.20A/B1-330[»]
2Z1BX-ray3.30A/B/C/D1-330[»]
ProteinModelPortaliP10518.
SMRiP10518. Positions 5-328.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10518.

Family & Domainsi

Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

eggNOGiCOG0113.
GeneTreeiENSGT00390000006998.
HOGENOMiHOG000020323.
HOVERGENiHBG001222.
InParanoidiP10518.
KOiK01698.
OMAiSGYFHPT.
OrthoDBiEOG751NFP.
PhylomeDBiP10518.
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.

P10518 [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:
EMBL
GenBank
DDBJ
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_006537639.1.
UniGeneiMm.6988.

Genome annotation databases

EnsembliENSMUST00000030090; ENSMUSP00000030090; ENSMUSG00000028393.
ENSMUST00000107444; ENSMUSP00000103068; ENSMUSG00000028393.
GeneIDi17025.
KEGGimmu:17025.
UCSCiuc008tez.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS18243.1.
PIRi S03187.
RefSeqi NP_001263375.1. NM_001276446.1.
NP_032551.3. NM_008525.4.
XP_006537702.1. XM_006537639.1.
UniGenei Mm.6988.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Z0I X-ray 3.20 A/B 1-330 [» ]
2Z1B X-ray 3.30 A/B/C/D 1-330 [» ]
ProteinModelPortali P10518.
SMRi P10518. Positions 5-328.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P10518. 5 interactions.
MINTi MINT-1869777.

PTM databases

PhosphoSitei P10518.

2D gel databases

REPRODUCTION-2DPAGE P10518.
SWISS-2DPAGE P10518.

Proteomic databases

MaxQBi P10518.
PaxDbi P10518.
PRIDEi P10518.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030090 ; ENSMUSP00000030090 ; ENSMUSG00000028393 .
ENSMUST00000107444 ; ENSMUSP00000103068 ; ENSMUSG00000028393 .
GeneIDi 17025.
KEGGi mmu:17025.
UCSCi uc008tez.1. mouse.

Organism-specific databases

CTDi 210.
MGIi MGI:96853. Alad.

Phylogenomic databases

eggNOGi COG0113.
GeneTreei ENSGT00390000006998.
HOGENOMi HOG000020323.
HOVERGENi HBG001222.
InParanoidi P10518.
KOi K01698.
OMAi SGYFHPT.
OrthoDBi EOG751NFP.
PhylomeDBi P10518.
TreeFami TF300665.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00318 .
Reactomei REACT_203298. Heme biosynthesis.

Miscellaneous databases

EvolutionaryTracei P10518.
NextBioi 291138.
PROi P10518.
SOURCEi Search...

Gene expression databases

Bgeei P10518.
CleanExi MM_ALAD.
ExpressionAtlasi P10518. baseline and differential.
Genevestigatori P10518.

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. "Cloning and sequence of mouse erythroid delta-aminolevulinate dehydratase cDNA."
    Bishop T.R., Hodes Z.I., Frelin L.P., Boyer S.H.
    Nucleic Acids Res. 17:1775-1775(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/c, C57BL/6J and DBA/2.
    Tissue: Placenta.
  3. "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].
    Strain: FVB/N.
    Tissue: Colon.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Crystal structure of 5-aminolevulinic acid dehydratase (ALAD) from Mus musculus."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).

Entry informationi

Entry nameiHEM2_MOUSE
AccessioniPrimary (citable) accession number: P10518
Secondary accession number(s): Q3THV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 29, 2014
This is version 129 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

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3