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Q59334 (HEM2_CHLP8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Ordered Locus Names:Cpar_0732
OrganismChlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp. thiosulfatophilum (strain DSM 263 / NCIB 8327)) [Complete proteome] [HAMAP]
Taxonomic identifier517417 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length328 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.

Catalytic activity

2 5-aminolevulinate = porphobilinogen + 2 H2O.

Enzyme regulation

Stimulated by magnesium, inhibited by zinc.

Pathway

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

Subunit structure

Homooctamer. Ref.3

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
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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

Chain1 – 328328Delta-aminolevulinic acid dehydratase
PRO_0000140499

Sites

Active site2001Schiff-base intermediate with substrate Ref.3 Ref.4
Active site2531Schiff-base intermediate with substrate Ref.3 Ref.4
Metal binding2381Magnesium
Binding site2101Substrate 1
Binding site2221Substrate 1
Binding site2791Substrate 2
Binding site3181Substrate 2

Secondary structure

...................................................... 328
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q59334 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D31B234328ABBE7B

FASTA32836,395
        10         20         30         40         50         60 
MSQLDLLNIV HRPRRLRRTA ALRNLVQENT LTVNDLVFPL FVMPGTNAVE EVSSMPGSFR 

        70         80         90        100        110        120 
FTIDRAVEEC KELYDLGIQG IDLFGIPEQK TEDGSEAYND NGILQQAIRA IKKAVPELCI 

       130        140        150        160        170        180 
MTDVALDPFT PFGHDGLVKD GIILNDETVE VLQKMAVSHA EAGADFVSPS DMMDGRIGAI 

       190        200        210        220        230        240 
REALDETDHS DVGILSYAAK YASSFYGPFR DALHSAPQFG DKSTYQMNPA NTEEAMKEVE 

       250        260        270        280        290        300 
LDIVEGADIV MVKPGLAYLD IVWRTKERFD VPVAIYHVSG EYAMVKAAAA KGWIDEDRVM 

       310        320 
MESLLCMKRA GADIIFTYYA KEAAKKLR 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of the Chlorobium vibrioforme hemB gene and characterization of its encoded enzyme, porphobilinogen synthase."
Rhie G.-E., Avissar Y.J., Beale S.I.
J. Biol. Chem. 271:8176-8182(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Chlorobaculum parvum NCIB 8327."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCIB 8327.
[3]"The X-ray structure of the plant like 5-aminolaevulinic acid dehydratase from Chlorobium vibrioforme complexed with the inhibitor laevulinic acid at 2.6 A resolution."
Coates L., Beaven G., Erskine P.T., Beale S.I., Avissar Y.J., Gill R., Mohammed F., Wood S.P., Shoolingin-Jordan P., Cooper J.B.
J. Mol. Biol. 342:563-570(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND LAEVULINIC ACID, ACTIVE SITE, SUBUNIT, ABSENCE OF CATALYTIC METAL COFACTOR.
[4]"Structure of Chlorobium vibrioforme 5-aminolaevulinic acid dehydratase complexed with a diacid inhibitor."
Coates L., Beaven G., Erskine P.T., Beale S.I., Wood S.P., Shoolingin-Jordan P.M., Cooper J.B.
Acta Crystallogr. D 61:1594-1598(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND 4,7-DIOXOSEBACIC ACID, ACTIVE SITE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38348 Genomic DNA. Translation: AAC43975.1.
CP001099 Genomic DNA. Translation: ACF11151.1.
RefSeqYP_001998351.1. NC_011027.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W1ZX-ray2.60A/B1-328[»]
2C1HX-ray2.60A/B1-328[»]
ProteinModelPortalQ59334.
SMRQ59334. Positions 10-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING517417.Cpar_0732.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF11151; ACF11151; Cpar_0732.
GeneID6419660.
KEGGcpc:Cpar_0732.
PATRIC21364722. VBIChlPar72705_0731.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
KOK01698.
OMAEVLCKMA.
OrthoDBEOG6VXFCB.

Enzyme and pathway databases

BioCycCPAR517417:GH95-761-MONOMER.
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...

Other

EvolutionaryTraceQ59334.

Entry information

Entry nameHEM2_CHLP8
AccessionPrimary (citable) accession number: Q59334
Secondary accession number(s): B3QMJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 14, 2014
This is version 83 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways