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Q43058 (HEM2_PHYPA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 74. 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
OrganismPhyscomitrella patens subsp. patens (Moss)
Taxonomic identifier3218 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaBryophytaBryophytinaBryopsidaFunariidaeFunarialesFunariaceaePhyscomitrella

Protein attributes

Sequence length430 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? – 430Delta-aminolevulinic acid dehydratase, chloroplasticPRO_0000013318

Sites

Active site2991Schiff-base intermediate with substrate By similarity
Active site3521Schiff-base intermediate with substrate By similarity
Metal binding3371Magnesium By similarity
Binding site3091Substrate 1 By similarity
Binding site3211Substrate 1 By similarity
Binding site3781Substrate 2 By similarity
Binding site4161Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q43058 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: FD1A477A28DEA399

FASTA43046,140
        10         20         30         40         50         60 
MVGVMMAAAA TPGCRVSQAL TACSSHEGLR RVAPVFGPGV VSVSAPCKLP RKLNVQAVAE 

        70         80         90        100        110        120 
PIAKSSPRTI EECEANVVAG NAPAAPPVPA KPSAPEGTPA ISPLVMPARP RRNRRSPALR 

       130        140        150        160        170        180 
AAFQETTISP ANFILPLFVH EGEQNAPIGA MPGCQRLGWR HGLIDEVYKA RDVGVNSVVL 

       190        200        210        220        230        240 
FPKVPDALKS STGDEAYNPD GLVPRCIRLL KAIPDLVIYT DVALDPYSSD GHDGIVREDG 

       250        260        270        280        290        300 
LIMNDETVHQ LCKQAVAQAQ AGADVVSPSD MMDGRVGAIR KALDLAGHQD VSIIAYTAKY 

       310        320        330        340        350        360 
ASAFYGPSRE ALDSNPRFGD KKTYQMNPAN YREALIETRM DEAEGADILM VKPAMPYLDV 

       370        380        390        400        410        420 
IRLLRDNTAL PISAYQVSGE YSMIRAGCRG MLDEKKAVLE SLLSIRRAGA DVILTYFAIQ 

       430 
AAQWLCAERV 

« Hide

References

[1]Gwarek M.A.
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89886 mRNA. Translation: CAA61978.1.
PIRS58169.

3D structure databases

ProteinModelPortalQ43058.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.

Enzyme and pathway databases

UniPathwayUPA00251; UER00318.

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_PHYPA
AccessionPrimary (citable) accession number: Q43058
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 22, 2014
This is version 74 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