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P77923 (HEM2_PROFF) 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
OrganismPropionibacterium freudenreichii subsp. freudenreichii
Taxonomic identifier66712 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length332 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.

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
   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: 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 – 332332Delta-aminolevulinic acid dehydratase
PRO_0000140506

Sites

Active site2011Schiff-base intermediate with substrate By similarity
Active site2531Schiff-base intermediate with substrate By similarity
Metal binding2381Magnesium By similarity
Binding site2111Substrate 1 By similarity
Binding site2221Substrate 1 By similarity
Binding site2791Substrate 2 By similarity
Binding site3181Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P77923 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 09FDDC7E45D216CB

FASTA33235,832
        10         20         30         40         50         60 
MADISIDPIV QRPRRLRRTP AIRRMVAETR LDPADLVLPM FAVEGLTEPR EIATMPGVWQ 

        70         80         90        100        110        120 
HTKESLQKAV HDAADAGVGA VMLFGTPLER DPIGSQAWNP HGILANAVRW AVEAEPELPV 

       130        140        150        160        170        180 
IADVCLDEFT DHGHCGVLAP DGTVDNDATL PLYAKMSVVL ADAGAAMLGP SGMMDGQIAV 

       190        200        210        220        230        240 
IRKALDDAGH TDTVLMAYSA KYASGFFGPF REAVDSQLKG DRRAYQQDPA NAIESLREIE 

       250        260        270        280        290        300 
LDLEQGADFV MVKPAMAYLD VLAAARAISN VPVAAYVVSG EYSMIEFAAK AGALDRKRCI 

       310        320        330 
MEALTSVKRA GASTIVTYWA TEVAIWLNEV RS 

« Hide

References

[1]Roessner C.A.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of the hemB gene encoding delta-aminolevulinic acid dehydratase from Propionibacterium freudenreichii."
Hashimoto Y., Yamashita Y., Ono H., Murooka Y.
J. Ferment. Bioeng. 82:93-100(1996)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 6207 / DSM 20271 / LMG 16412 / NBRC 12424 / NCIMB 5959 / NCTC 10470 / NRRL B-3523.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U51164 Genomic DNA. Translation: AAB07863.1.
D85417 Genomic DNA. Translation: BAA21911.1.

3D structure databases

ProteinModelPortalP77923.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_PROFF
AccessionPrimary (citable) accession number: P77923
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
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