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Q59643

- HEM2_PSEAE

UniProt

Q59643 - HEM2_PSEAE

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Protein
Delta-aminolevulinic acid dehydratase
Gene
hemB, PA5243
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

2 5-aminolevulinate = porphobilinogen + 2 H2O.1 Publication

Enzyme regulationi

Stimulated by magnesium ions.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei205 – 2051Schiff-base intermediate with substrate2 Publications
Binding sitei215 – 2151Substrate 1
Binding sitei229 – 2291Substrate 1
Metal bindingi245 – 2451Magnesium
Active sitei260 – 2601Schiff-base intermediate with substrate2 Publications
Binding sitei286 – 2861Substrate 2
Binding sitei324 – 3241Substrate 2

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. porphobilinogen synthase activity Source: PseudoCAP

GO - Biological processi

  1. porphyrin-containing compound biosynthetic process Source: PseudoCAP
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00251; UER00318.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
Short name:
ALAD
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
Gene namesi
Name:hemB
Ordered Locus Names:PA5243
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA5243.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Delta-aminolevulinic acid dehydratase
PRO_0000140507Add
BLAST

Interactioni

Subunit structurei

Homooctamer; formed by oligomerization of dimers.1 Publication

Protein-protein interaction databases

STRINGi208964.PA5243.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni10 – 123
Turni15 – 195
Helixi22 – 287
Helixi35 – 373
Beta strandi38 – 4912
Beta strandi51 – 533
Beta strandi61 – 644
Helixi65 – 7713
Beta strandi82 – 876
Helixi91 – 933
Beta strandi95 – 973
Helixi99 – 1024
Helixi107 – 11812
Beta strandi122 – 1287
Turni131 – 1333
Beta strandi134 – 1363
Helixi150 – 16617
Beta strandi170 – 1745
Helixi181 – 19111
Beta strandi198 – 2069
Helixi209 – 2113
Helixi212 – 2165
Helixi221 – 2244
Helixi229 – 2313
Beta strandi232 – 2343
Helixi240 – 25112
Beta strandi255 – 2617
Helixi263 – 2653
Helixi266 – 27611
Beta strandi280 – 2845
Helixi286 – 29712
Helixi305 – 31612
Beta strandi319 – 3235
Helixi326 – 3349

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ59643.
SMRiQ59643. Positions 10-335.

Miscellaneous databases

EvolutionaryTraceiQ59643.

Family & Domainsi

Sequence similaritiesi

Belongs to the ALADH family.

Phylogenomic databases

eggNOGiCOG0113.
HOGENOMiHOG000020323.
KOiK01698.
OMAiMTILTHR.
OrthoDBiEOG6VXFCB.
PhylomeDBiQ59643.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view]
PANTHERiPTHR11458. PTHR11458. 1 hit.
PfamiPF00490. ALAD. 1 hit.
[Graphical view]
PIRSFiPIRSF001415. Porphbilin_synth. 1 hit.
PRINTSiPR00144. DALDHYDRTASE.
SMARTiSM01004. ALAD. 1 hit.
[Graphical view]
PROSITEiPS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59643-1 [UniParc]FASTAAdd to Basket

« Hide

MSFTPANRAY PYTRLRRNRR DDFSRRLVRE NVLTVDDLIL PVFVLDGVNQ    50
RESIPSMPGV ERLSIDQLLI EAEEWVALGI PALALFPVTP VEKKSLDAAE 100
AYNPEGIAQR ATRALRERFP ELGIITDVAL DPFTTHGQDG ILDDDGYVLN 150
DVSIDVLVRQ ALSHAEAGAQ VVAPSDMMDG RIGAIREALE SAGHTNVRIM 200
AYSAKYASAY YGPFRDAVGS ASNLGKGNKA TYQMDPANSD EALHEVAADL 250
AEGADMVMVK PGMPYLDIVR RVKDEFRAPT FVYQVSGEYA MHMGAIQNGW 300
LAESVILESL TAFKRAGADG ILTYFAKQAA EQLRRGR 337
Length:337
Mass (Da):37,037
Last modified:November 1, 1996 - v1
Checksum:i7D650C49795D542C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X91820 Genomic DNA. Translation: CAA62930.1.
AE004091 Genomic DNA. Translation: AAG08628.1.
PIRiS60577.
RefSeqiNP_253930.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG08628; AAG08628; PA5243.
GeneIDi879701.
KEGGipae:PA5243.
PATRICi19845337. VBIPseAer58763_5495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X91820 Genomic DNA. Translation: CAA62930.1 .
AE004091 Genomic DNA. Translation: AAG08628.1 .
PIRi S60577.
RefSeqi NP_253930.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B4K X-ray 1.67 A/B 1-337 [» ]
1GZG X-ray 1.66 A/B 1-337 [» ]
1W54 X-ray 2.20 A/B 1-337 [» ]
1W56 X-ray 1.70 A/B 1-337 [» ]
1W5M X-ray 1.60 A/B 1-337 [» ]
1W5N X-ray 1.65 A/B 1-337 [» ]
1W5O X-ray 1.85 A/B 1-337 [» ]
1W5P X-ray 1.55 A/B 1-337 [» ]
1W5Q X-ray 1.40 A/B 1-337 [» ]
2C13 X-ray 2.15 A/B 1-337 [» ]
2C14 X-ray 1.90 A/B 1-337 [» ]
2C15 X-ray 1.48 A/B 1-337 [» ]
2C16 X-ray 2.02 A/B 1-337 [» ]
2C18 X-ray 1.93 A/B 1-337 [» ]
2C19 X-ray 2.05 A/B 1-337 [» ]
2WOQ X-ray 1.75 A 1-337 [» ]
ProteinModelPortali Q59643.
SMRi Q59643. Positions 10-335.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA5243.

Protocols and materials databases

DNASUi 879701.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG08628 ; AAG08628 ; PA5243 .
GeneIDi 879701.
KEGGi pae:PA5243.
PATRICi 19845337. VBIPseAer58763_5495.

Organism-specific databases

PseudoCAPi PA5243.

Phylogenomic databases

eggNOGi COG0113.
HOGENOMi HOG000020323.
KOi K01698.
OMAi MTILTHR.
OrthoDBi EOG6VXFCB.
PhylomeDBi Q59643.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00318 .

Miscellaneous databases

EvolutionaryTracei Q59643.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR001731. Porphobilinogen_synth.
[Graphical view ]
PANTHERi PTHR11458. PTHR11458. 1 hit.
Pfami PF00490. ALAD. 1 hit.
[Graphical view ]
PIRSFi PIRSF001415. Porphbilin_synth. 1 hit.
PRINTSi PR00144. DALDHYDRTASE.
SMARTi SM01004. ALAD. 1 hit.
[Graphical view ]
PROSITEi PS00169. D_ALA_DEHYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiHEM2_PSEAE
AccessioniPrimary (citable) accession number: Q59643
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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