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P43087 (HEM2_SYNE7) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 79. 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
Ordered Locus Names:Synpcc7942_1792
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 1 zinc ion per monomer By similarity.

Pathway

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

Subunit structure

Homooctamer By similarity.

Sequence similarities

Belongs to the ALADH family.

Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   LigandMagnesium
Metal-binding
Zinc
   Molecular functionLyase
   Technical termComplete 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 – 326326Delta-aminolevulinic acid dehydratase
PRO_0000140520

Sites

Active site1981Schiff-base intermediate with substrate By similarity
Active site2511Schiff-base intermediate with substrate By similarity
Metal binding1191Zinc; catalytic By similarity
Metal binding1211Zinc; catalytic By similarity
Metal binding1291Zinc; catalytic By similarity
Metal binding2361Magnesium By similarity
Binding site2081Substrate 1 By similarity
Binding site2201Substrate 1 By similarity
Binding site2771Substrate 2 By similarity
Binding site3161Substrate 2 By similarity

Experimental info

Sequence conflict2871A → R in CAA49892. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P43087 [UniParc].

Last modified April 18, 2006. Version 2.
Checksum: 0C4F44658CEB37BF

FASTA32635,574
        10         20         30         40         50         60 
MFPTHRPRRL RSSETLRRMV RETTLTSADF IYPLFAVPGE GVAKEVTSMP GVYQLSIDKI 

        70         80         90        100        110        120 
VEEAKEVYDL GIPSIILFGI PTDKDNDATG AWHDCGIVQK AATAVKEAVP ELIVAADTCL 

       130        140        150        160        170        180 
CEYTPHGHCG YLEVGDLSGR VLNDPTLELL RKTAVSQAKA GADIIAPSGM MDGFVATIRD 

       190        200        210        220        230        240 
ALDEAGFSDT PIMAYSAKYA SAYYGPFRDA AESTPQFGDR RTYQMDPGNS REALKEVELD 

       250        260        270        280        290        300 
VAEGADIVMV KPALSYMDII CRIKETTDLP VAAYNVSGEY SMVKAAALNG WIDEERVVLE 

       310        320 
TLTSFKRAGA DLILTYHAKD AARWLA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterisation of genes for tetrapyrrole biosynthesis from the cyanobacterium Anacystis nidulans R2."
Jones M.C., Jenkins J.M., Smith A.G., Howe C.J.
Plant Mol. Biol. 24:435-448(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7942.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70434 Genomic DNA. Translation: CAA49892.1.
CP000100 Genomic DNA. Translation: ABB57822.1.
RefSeqYP_400809.1. NC_007604.1.

3D structure databases

ProteinModelPortalP43087.
SMRP43087. Positions 5-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1140.Synpcc7942_1792.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB57822; ABB57822; Synpcc7942_1792.
GeneID3774367.
KEGGsyf:Synpcc7942_1792.
PATRIC23789009. VBISynElo51371_2028.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
KOK01698.
OrthoDBEOG6VXFCB.
ProtClustDBPRK09283.

Enzyme and pathway databases

BioCycSYNEL:SYNPCC7942_1792-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...

Entry information

Entry nameHEM2_SYNE7
AccessionPrimary (citable) accession number: P43087
Secondary accession number(s): Q31M97
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 18, 2006
Last modified: November 13, 2013
This is version 79 of the entry and version 2 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