Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q42682 (HEM2_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 72. 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
OrganismChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 stroma

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   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 – 2424Chloroplast Potential
Chain25 – 390366Delta-aminolevulinic acid dehydratase, chloroplastic
PRO_0000013315

Sites

Active site2511Schiff-base intermediate with substrate By similarity
Active site3121Schiff-base intermediate with substrate By similarity
Metal binding2971Magnesium By similarity
Binding site2611Substrate 1 By similarity
Binding site2811Substrate 1 By similarity
Binding site3381Substrate 2 By similarity
Binding site3771Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q42682 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 6114C4E0325A4242

FASTA39043,046
        10         20         30         40         50         60 
MQMMQRNVVG QRPVAGSRRS LVVANVAEVT RPAVSTNGKH RTGVPEGTPI VTPQDLPSRP 

        70         80         90        100        110        120 
RRNRRSESFR ASVREVNVSP ANFILPIFIH EESNQNVPIA SMPGINRLAY GKNVIDYVAE 

       130        140        150        160        170        180 
PRSYGVNQVV VFPKTPDHLK TQTAEEAFNK NGLSQRTIRL LKDSFPDLEV YTDVALDPYN 

       190        200        210        220        230        240 
SDGHDGIVSD AGVILNDETI EYLCRQAVSQ AEAGADVVSP SDMMDGRVGA IRRALDREGF 

       250        260        270        280        290        300 
TNVSIMSYTA KYASAYYGPF RDALASAPKP GQAHRRIPPN KKTYQMDPAN YREAIREAKA 

       310        320        330        340        350        360 
DEAEGADIMM VKPGMPYLDV VRLLRETSPL PVAVYHVSGE YAMLKAAAER GWLNEKDAVL 

       370        380        390 
EAMTCFRRAG GDLILTYYGI EASKWLAGEK 

« Hide

References

[1]"Structure and expression of the Chlamydomonas reinhardtii alad gene encoding the chlorophyll biosynthetic enzyme, delta-aminolevulinic acid dehydratase (porphobilinogen synthase)."
Matters G.L., Beale S.I.
Plant Mol. Biol. 27:607-617(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: NO-.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U19876 mRNA. Translation: AAA79515.1.
PIRS53487.

3D structure databases

ProteinModelPortalQ42682.
SMRQ42682. Positions 58-387.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ42682.
ProMEXQ42682.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0113.

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]
PIRSFPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSPR00144. DALDHYDRTASE.
SMARTSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM2_CHLRE
AccessionPrimary (citable) accession number: Q42682
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 72 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