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Q59643 (HEM2_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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:PA5243
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length337 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 By similarity.

Catalytic activity

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

Enzyme regulation

Stimulated by magnesium ions.

Pathway

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

Subunit structure

Homooctamer; formed by oligomerization of dimers. Ref.3

Sequence similarities

Belongs to the ALADH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Delta-aminolevulinic acid dehydratase
PRO_0000140507

Sites

Active site2051Schiff-base intermediate with substrate Ref.4 Ref.5
Active site2601Schiff-base intermediate with substrate Ref.4 Ref.5
Metal binding2451Magnesium
Binding site2151Substrate 1
Binding site2291Substrate 1
Binding site2861Substrate 2
Binding site3241Substrate 2

Secondary structure

............................................................... 337
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q59643 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7D650C49795D542C

FASTA33737,037
        10         20         30         40         50         60 
MSFTPANRAY PYTRLRRNRR DDFSRRLVRE NVLTVDDLIL PVFVLDGVNQ RESIPSMPGV 

        70         80         90        100        110        120 
ERLSIDQLLI EAEEWVALGI PALALFPVTP VEKKSLDAAE AYNPEGIAQR ATRALRERFP 

       130        140        150        160        170        180 
ELGIITDVAL DPFTTHGQDG ILDDDGYVLN DVSIDVLVRQ ALSHAEAGAQ VVAPSDMMDG 

       190        200        210        220        230        240 
RIGAIREALE SAGHTNVRIM AYSAKYASAY YGPFRDAVGS ASNLGKGNKA TYQMDPANSD 

       250        260        270        280        290        300 
EALHEVAADL AEGADMVMVK PGMPYLDIVR RVKDEFRAPT FVYQVSGEYA MHMGAIQNGW 

       310        320        330 
LAESVILESL TAFKRAGADG ILTYFAKQAA EQLRRGR 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, mapping and functional characterization of the hemB gene of Pseudomonas aeruginosa, which encodes a magnesium-dependent 5-aminolevulinic acid dehydratase."
Frankenberg N., Kittel T., Hungerer C., Roemling U., Jahn D.
Mol. Gen. Genet. 257:485-489(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[3]"High resolution crystal structure of a Mg(2+)-dependent porphobilinogen synthase."
Frankenberg N., Erskine P.T., Cooper J.B., Shoolingin-Jordan P.M., Jahn D., Heinz D.W.
J. Mol. Biol. 289:591-602(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH LEVULINIC ACID AND MAGNESIUM, SUBUNIT.
[4]"Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism."
Frere F., Schubert W.-D., Stauffer F., Frankenberg N., Neier R., Jahn D., Heinz D.W.
J. Mol. Biol. 320:237-247(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF MUTANT ASN-139 IN COMPLEX WITH 5-FLUOROLEVULINIC ACID AND MAGNESIUM, COFACTOR, ACTIVE SITE.
[5]"Probing the active site of Pseudomonas aeruginosa porphobilinogen synthase using newly developed inhibitors."
Frere F., Nentwich M., Gacond S., Heinz D.W., Neier R., Frankenberg-Dinkel N.
Biochemistry 45:8243-8253(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM; 5-HYDROXYLEVULINIC ACID AND OTHER INHIBITORS, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE.
[6]"Structure of the heme biosynthetic Pseudomonas aeruginosa porphobilinogen synthase in complex with the antibiotic alaremycin."
Heinemann I.U., Schulz C., Schubert W.D., Heinz D.W., Wang Y.G., Kobayashi Y., Awa Y., Wachi M., Jahn D., Jahn M.
Antimicrob. Agents Chemother. 54:267-272(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ALAREMYCIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91820 Genomic DNA. Translation: CAA62930.1.
AE004091 Genomic DNA. Translation: AAG08628.1.
PIRS60577.
RefSeqNP_253930.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4KX-ray1.67A/B1-337[»]
1GZGX-ray1.66A/B1-337[»]
1W54X-ray2.20A/B1-337[»]
1W56X-ray1.70A/B1-337[»]
1W5MX-ray1.60A/B1-337[»]
1W5NX-ray1.65A/B1-337[»]
1W5OX-ray1.85A/B1-337[»]
1W5PX-ray1.55A/B1-337[»]
1W5QX-ray1.40A/B1-337[»]
2C13X-ray2.15A/B1-337[»]
2C14X-ray1.90A/B1-337[»]
2C15X-ray1.48A/B1-337[»]
2C16X-ray2.02A/B1-337[»]
2C18X-ray1.93A/B1-337[»]
2C19X-ray2.05A/B1-337[»]
2WOQX-ray1.75A1-337[»]
ProteinModelPortalQ59643.
SMRQ59643. Positions 10-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA5243.

Protocols and materials databases

DNASU879701.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID879701.
KEGGpae:PA5243.
PATRIC19845337. VBIPseAer58763_5495.

Organism-specific databases

PseudoCAPPA5243.

Phylogenomic databases

eggNOGCOG0113.
HOGENOMHOG000020323.
KOK01698.
OMAGEYAMVE.
OrthoDBEOG6VXFCB.
ProtClustDBPRK09283.

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...

Other

EvolutionaryTraceQ59643.

Entry information

Entry nameHEM2_PSEAE
AccessionPrimary (citable) accession number: Q59643
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 106 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