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Q42836 (HEM2_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Delta-aminolevulinic acid dehydratase, chloroplastic

Short name=ALADH
EC=4.2.1.24
Alternative name(s):
Porphobilinogen synthase
Gene names
Name:HEMB
Synonyms:ALAD
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Cofactor

Binds 2 magnesium ions per monomer. The first magnesium ion is required for catalysis. The second functions as allosteric activator By similarity.

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.

Subunit structure

Homooctamer By similarity.

Subcellular location

Plastidchloroplast.

Sequence similarities

Belongs to the ALADH family.

Ontologies

Keywords
   Biological processChlorophyll biosynthesis
Heme biosynthesis
Porphyrin biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical termAllosteric enzyme
Gene Ontology (GO)
   Biological_processchlorophyll biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

protoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

porphobilinogen synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Chloroplast Potential
Chain? – 428Delta-aminolevulinic acid dehydratase, chloroplasticPRO_0000013316

Sites

Active site2941Schiff-base intermediate with substrate By similarity
Active site3471Schiff-base intermediate with substrate By similarity
Metal binding3321Magnesium By similarity
Binding site3041Substrate 1 By similarity
Binding site3161Substrate 1 By similarity
Binding site3731Substrate 2 By similarity
Binding site4121Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q42836 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2E3F6C37109816F7

FASTA42846,213
        10         20         30         40         50         60 
MASTVPFSPA KVQMFQATNC HGHAGFGSSF AVPRTGPRPR SVAVRVSSEQ EAAATVRAPS 

        70         80         90        100        110        120 
GRSIEECEAD AVAGRFPAPS CVCQTPKAPD GTPEIRPLDM AKRPRRNRRS PALRAAFQET 

       130        140        150        160        170        180 
SISPANLVLP LFIHEGEEDA PIGAMPGCFR LGWQHGLLAE VYKARDVGVN SFVLFPKVPD 

       190        200        210        220        230        240 
ALKSPTGVEA YNDNGLVPRT IRLLKDKFPD IIVYTDVALD PYSSDGHDGI VRKDGVILND 

       250        260        270        280        290        300 
ETVYQLCKQA VSQARAGADV VSPSNMMDGR VGAIRSALDA EGFNDVSIMS YTAKYASSFY 

       310        320        330        340        350        360 
GPFREALDSN PRFGDKKTYQ MNPANYREAL LETAADEAEG ADILLVKPGL PYLDIIRLSR 

       370        380        390        400        410        420 
DNSALPIAAY QVSGEYSMIK AGGALNMIDE EKVMMESLMC LRRAGADVIL TYFARQPPAV 


LCGMGTAK 

« Hide

References

[1]Bougri O.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Bonus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92402 mRNA. Translation: CAA63139.1.
PIRT04472.

3D structure databases

ProteinModelPortalQ42836.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ42836.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneQ42836.

Enzyme and pathway databases

UniPathwayUPA00251; UER00318.

Gene expression databases

GenevestigatorQ42836.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERPTHR11458. PTHR11458. 1 hit.
PfamPF00490. ALAD. 1 hit.
[Graphical view]
PRINTSPR00144. DALDHYDRTASE.
SMARTSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM2_HORVU
AccessionPrimary (citable) accession number: Q42836
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 16, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways