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P42504 (HEM2_RHOCA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 64. 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

Short name=ALAD
Short name=ALADH
EC=4.2.1.24
Alternative name(s):
Porphobilinogen synthase
Gene names
Name:hemB
OrganismRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifier1061 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
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. Ref.2

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O. Ref.2

Pathway

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

Subunit structure

Homohexamer. Ref.2

Miscellaneous

Does not seem to have a metal requirement for activity.

Sequence similarities

Belongs to the ALADH family.

Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   Molecular functionLyase
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: InterPro

porphobilinogen synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Delta-aminolevulinic acid dehydratase
PRO_0000140508

Sites

Active site2021Schiff-base intermediate with substrate By similarity
Active site2561Schiff-base intermediate with substrate By similarity
Binding site2121Substrate 1 By similarity
Binding site2251Substrate 1 By similarity
Binding site2821Substrate 2 By similarity
Binding site3211Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P42504 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 4118DED5A15C8DBE

FASTA33235,854
        10         20         30         40         50         60 
MTLITPPFPT NRLRRMRRTE ALRDLAQENR LSVKDLIWPI FITDVPGADV EISSMPGVVR 

        70         80         90        100        110        120 
RTMDGALKAA EGSRDAGHSR DLPVPLTDPA VKTETCEMAW QPDNFTNRVI AAMKQAVPEV 

       130        140        150        160        170        180 
AIMTDIALDP YNANGHDGLV RDGILLNDET TEALVKMALA QAAAGADILG PSDMMDGRVG 

       190        200        210        220        230        240 
AIRQAMEAAG HKDIAILSYA AKYASAFYGP FRDAVGASSA LKGDKKTYQM NPANSAEALR 

       250        260        270        280        290        300 
NVARDIAEGA DMVMVKPGMP YLDIVRQVKD AFGMPTYAYQ VSGEYAMLMA AVQNGWLNHD 

       310        320        330 
KVMLESLMAF RRAGCDGVLT YFAPAAAKLI GA 

« Hide

References

[1]"Nucleotide sequence of the Rhodobacter capsulatus hemB gene."
Indest K., Biel A.J.
Plant Physiol. 108:421-421(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PAS100.
[2]"Rhodobacter capsulatus porphobilinogen synthase, a high activity metal ion independent hexamer."
Bollivar D.W., Clauson C., Lighthall R., Forbes S., Kokona B., Fairman R., Kundrat L., Jaffe E.K.
BMC Biochem. 5:17-17(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, ABSENCE OF METAL COFACTOR REQUIREMENT, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14593 Genomic DNA. Translation: AAA92884.1.

3D structure databases

ProteinModelPortalP42504.
SMRP42504. Positions 8-331.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13250.
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_RHOCA
AccessionPrimary (citable) accession number: P42504
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways