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P54919 (HEM2_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 91. 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:SCO3311
ORF Names:SCE68.09c
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group

Protein attributes

Sequence length330 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
   Technical termComplete proteome
Reference 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 – 330330Delta-aminolevulinic acid dehydratase
PRO_0000140519

Sites

Active site2031Schiff-base intermediate with substrate By similarity
Active site2551Schiff-base intermediate with substrate By similarity
Metal binding2401Magnesium By similarity
Binding site2131Substrate 1 By similarity
Binding site2241Substrate 1 By similarity
Binding site2811Substrate 2 By similarity
Binding site3201Substrate 2 By similarity

Experimental info

Sequence conflict1001D → V in AAA61398. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54919 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: D2AF1F8B971F30F5

FASTA33035,453
        10         20         30         40         50         60 
MTTYGSFPGA RPRRLRTTPV MRRMVAETRL HPADFILPAF VREGVSEPVP IAAMPGVVQH 

        70         80         90        100        110        120 
TRDTLKKAAA EAVEAGVSGI MLFGVPEDGK KDAAGTAGTD PDGILQVALR DVRAEVGDEL 

       130        140        150        160        170        180 
LVMSDLCLDE FTDHGHCGVL DGQGRVDNDA TLERYAEMAQ VQADAGAHVV GPSGMMDGQI 

       190        200        210        220        230        240 
GVIRDALDQI GREDVAILAY TAKYASAFYG PFREAVGSSL KGDRKTYQQD SANARESLRE 

       250        260        270        280        290        300 
LALDLEEGAD MVMVKPAGPY LDILAKVAEA SDVPVAAYQI SGEYSMIEAA AEKGWIDRDR 

       310        320        330 
AILESLTGIK RAGARNILTY WATEVARTLR 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterisation of the genes that encode enzymes for first steps of tetrapyrrole biosynthesis in Streptomyces coelicolor A3(2)."
Petricek M.
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A3(2) / NRRL B-16638.
[2]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U19249 Genomic DNA. Translation: AAA61398.1.
AL939116 Genomic DNA. Translation: CAB45345.1.
PIRT36259.
RefSeqNP_627521.1. NC_003888.3.

3D structure databases

ProteinModelPortalP54919.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO3311.

Proteomic databases

PRIDEP54919.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB45345; CAB45345; CAB45345.
GeneID1098745.
KEGGsco:SCO3311.
PATRIC23736366. VBIStrCoe124346_3371.

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
KOK01698.
OMADMILTYF.
OrthoDBEOG6VXFCB.
PhylomeDBP54919.

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_STRCO
AccessionPrimary (citable) accession number: P54919
Secondary accession number(s): Q9S2E6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: May 14, 2014
This is version 91 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