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Reviewed, UniProtKB/Swiss-Prot P10518 (HEM2_MOUSE)

Last modified January 19, 2010. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Delta-aminolevulinic acid dehydratase
      Short name=ALADH
    EC=4.2.1.24
Alternative name(s):
    Porphobilinogen synthase
Gene names
Name: Alad
Synonyms: Lv
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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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.

Sequence similarities

Belongs to the ALADH family.

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Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processheme biosynthetic process

Inferred from direct assay. Source: MGI

   Molecular functionidentical protein binding

Inferred from physical interaction. Source: MGI

porphobilinogen synthase activity

Inferred from direct assay. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Delta-aminolevulinic acid dehydratase
PRO_0000140528

Sites

Active site2521 By similarity
Metal binding1221Zinc; catalytic By similarity
Metal binding1241Zinc; catalytic By similarity
Metal binding1321Zinc; catalytic By similarity

Secondary structure

1 .................................................. 330
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P10518-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 84052DC911C153EB

FASTA33036,024
        10         20         30         40         50         60 
MHHQSVLHSG YFHPLLRSWQ TAASTVSASN LIYPIFVTDV PDDVQPIASL PGVARYGVNQ 

        70         80         90        100        110        120 
LEEMLRPLVE AGLRCVLIFG VPSRVPKDEQ GSAADSEDSP TIEAVRLLRK TFPSLLVACD 

       130        140        150        160        170        180 
VCLCPYTSHG HCGLLSENGA FLAEESRQRL AEVALAYAKA GCQVVAPSDM MDGRVEAIKA 

       190        200        210        220        230        240 
ALLKHGLGNR VSVMSYSAKF ASCFYGPFRD AAQSSPAFGD RRCYQLPPGA RGLALRAVAR 

       250        260        270        280        290        300 
DIQEGADMLM VKPGLPYLDM VREVKDKHPE LPLAVYQVSG EFAMLWHGAQ AGAFDLRTAV 

       310        320        330 
LETMTAFRRA GADIIITYFA PQLLKWLKEE

« Hide

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References

« Hide 'large scale' references
[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: 2922298] [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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00112719.
PIRS03187.
RefSeqNP_032551.3.
UniGeneMm.6988

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z0IX-ray3.20A/B1-330[»]
2Z1BX-ray3.30A/B/C/D1-330[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP10518.

PTM databases

PhosphoSiteP10518.

2-D gel databases

SWISS-2DPAGEP10518.
REPRODUCTION-2DPAGEP10518.

Proteomic databases

PRIDEP10518.

Genome annotation databases

EnsemblENSMUST00000030090; ENSMUSP00000030090; ENSMUSG00000028393; Mus musculus. [Genome view]
ENSMUST00000107444; ENSMUSP00000103068; ENSMUSG00000028393; Mus musculus. [Genome view]
GeneID17025.
KEGGmmu:17025.
NMPDRfig|10090.3.peg.9704.
UCSCuc008tez.1. mouse.

Organism-specific databases

CTD17025.
MGIMGI:96853. Alad.

Phylogenomic databases

HOGENOMHBG285270.
HOVERGENP10518.
InParanoidP10518.
OMADPFTSHG.
OrthoDBEOG9DFS6V.
PhylomeDBP10518.

Enzyme and pathway databases

BRENDA4.2.1.24. 244.

Gene expression databases

ArrayExpressP10518.
BgeeP10518.
CleanExMM_ALAD.
GenevestigatorP10518.
GermOnlineENSMUSG00000028393. Mus musculus.

Family and domain databases

InterProIPR001731. 4pyrrol_synth_porphobiln_synth.
IPR013785. Aldolase_TIM.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR11458. AlaD_dehydratase. 1 hit.
PfamPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSPR00144. DALDHYDRTASE.
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio291138.
SOURCESearch...

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Entry information

Entry nameHEM2_MOUSE
AccessionPrimary (citable) accession number: P10518
Secondary accession number(s): Q3THV6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 19, 2010
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents